Dissertations / Theses on the topic 'Common carp'
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Hung, Ching Yee. "Survival strategies of common carp, cyprinus carpio, during prolonged starvation and hypoxia /." access full-text access abstract and table of contents, 2005. http://libweb.cityu.edu.hk/cgi-bin/ezdb/thesis.pl?phd-bch-b19887346a.pdf.
Full text"Submitted to Department of Biology and Chemistry in partial fulfillment of the requirements for the degree of Doctor of Philosophy." Includes bibliographical references (leaves 233-269).
Williams, Paul Edwin. "Evaluation of a Common Carp (Cyprinus carpio L.) Exclusion and Trapping Device for Use in Aquatic Plant Founder Colony Establishment." Thesis, University of North Texas, 2008. https://digital.library.unt.edu/ark:/67531/metadc6038/.
Full textCopeland, Donald Lee. "Production of Recombinant Carp Leptin and its Effects on Lipid Metabolism in the Common Carp (Cyprinus Carpio)." University of Akron / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=akron1342135953.
Full textMacCarthy, Eugene. "Pentraxins and the acute phase response in common carp Cyprinus carpio." Thesis, Keele University, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.436139.
Full text周楚穎 and Chor-wing Vivian Ng. "Characterization and sequencing of sex hormone-binding globulin in common carp (cyprinus carpio)." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2000. http://hub.hku.hk/bib/B31224982.
Full textNinh, Nguyen Huu. "Communal or separate rearing of families in selective breeding of common carp (Cyprinus carpio L.)." Thesis, University of Stirling, 2009. http://hdl.handle.net/1893/1638.
Full textHoltan, Marte Berg. "Plasma melatonin profiles in Common carp (Cyprinus carpio) exposed to indoor photoperiods." Thesis, Norges teknisk-naturvitenskapelige universitet, Institutt for biologi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:no:ntnu:diva-13699.
Full textChakraborty, Subhash Chandra. "Energy budget and aspects of energy metabolism in common carp, Cyprinus carpio." Thesis, University of Stirling, 1992. http://hdl.handle.net/1893/1808.
Full textSilva, Roberto de Souza Gomes da. "Obtenção de gelatina utilizando cabeças de carpa comum (Cyprinus carpio): avaliação das etapas de pré-tratamento e extração." reponame:Repositório Institucional da FURG, 2010. http://repositorio.furg.br/handle/1/2574.
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A carpa comum (Cyprinus carpio) é conhecida por ser geradora de quantidade considerável de rejeitos mal aproveitados por indústrias pesqueiras. Estes rejeitos são constituídos por vísceras, peles, ossos e cabeças. Diversos fatores têm contribuído para a utilização de cabeças de carpa provenientes da industrialização, dentre estes a quantidade de cabeças desperdiçadas, que pode atingir 22% do volume da matériaprima, e é uma fonte de nutrientes de baixo custo e rica em colágeno. A maioria das gelatinas comerciais é derivada de mamíferos, sendo peles e ossos de bovinos e suínos as principais matérias-primas do produto. A gelatina é de uma proteína pura, digestível, que se obtém a partir da hidrólise à quente do colágeno, e por este motivo, o pescado torna-se uma potencial fonte de matéria-prima. A aplicação da gelatina é diversificada, podendo ser utilizada na indústria cosmética, farmacêutica,fotográfica e alimentícia. O presente estudo foi dividido em dois objetivos. Primeiramente foram avaliados os efeitos da concentração alcalina, tempo de pré-tratamento e prétratamentos com ou sem troca de solução alcalina do material para a obtenção de gelatina das peles das cabeças de carpa. Foi utilizado um planejamento fatorial 23 completo, e os fatores de estudo foram concentração de NaOH (3-4 M), tempo de prétratamento(45-105 min), e troca de solução de NaOH no pré-tratamento, tendo como respostas rendimento em gelatina, força do gel e ponto de fusão. Na segunda etapa, os ossos remanescentes deste processo foram utilizados para o estudo da influência da granulometria (1-2 mm) nas respostas consideradas das gelatinas extraídas da fração óssea, através da comparação das médias pela aplicação do teste de Tukey, com intervalo de 95% de confiança. Foram realizadas quatro extrações com pH e temperaturas de cada extração de 5,3-60°C, 4,4-70°C, 3,8-80°C e 3,6-85°C. Para as gelatinas extraídas das peles, o maior rendimento (2,27%) foi obtido com solução de NaOH 3 M, 45 min e sem troca de solução no pré-tratamento. Os maiores valores de força do gel (298,7 g) e ponto de fusão (29°C) foram obtidos a concentração de solução NaOH 3 M, 45 min e sem troca de solução alcalina. Para as gelatinas extraídas dos ossos, o maior rendimento (4,86%) foi obtido na granulometria de 1 mm. Os maiores valores de força do gel (128,2 e 131,5 g) não apresentaram diferença significativa (p≤0,05) e foram encontrados na primeira extração das granulometrias de 1 e 2 mm, respectivamente. Na fração óssea a 2 mm, se obteve o maior ponto de fusão, sendo 28,5°C na a primeira extração. O rendimento total da gelatina obtida a partir das cabeças de carpa foi de 7,13%.
Common carp (Cyprinus carpio) is known to produce large amount of byproduct does not made use for fisheries industries. These byproduct can be viscera, skin, bone and head, all riches in collagen. Several factors have been contributing to the use of the carp head coming from industrialization, among which the amount of carp head wasted, with which it can reach around 22% of the volume of the raw material, and it is a source of low costs nutrients. Most of commercial gelatin is derived from mammalian, being skins and bones of bovine and porcine the main raw material of this foodstuff. Gelatin is a pure and digestible protein, which is obtained from hydrolysis of the collagen, and for this reason, the fish become a potential source from raw material. Its application is branched out, being able to used in the cosmetic, pharmaceutical, photographic and food industries. The present study was divided into two parts. At first, it was valued the effect of alkaline concentration, pre-treatment time of the raw material, and treatment with and without change of alkaline solution, in the process of extraction of skin/muscles fraction gelatin of carp head coming from manufacturing processing of this fish. It was used 23 complete experimental design. Pre-treatment time (45-105 min), concentration of alkaline solution (3-4 M) and pre-treatment with change of alkaline solution were chosen as independent variable. Gelatin yield, gel strength and melting point were the response variable. At the second part, was valued of the influence of the bones granulometry (1-2 mm), remaining of the skin extraction of common carp head, in the gelatin yield, gel strength and melting point through the average results comparison by the Tukey test, where differences were considered significant at p≤0.05. It was used four extraction with pH and temperature of each extraction 5.3-60°C, 4.4-70°C, 3.8-80°C and 3.6-85°C. To the skin gelatin the higher gelatin yield (2.27%) was obtained with NaOH solution 3 M, 45 min and pre-treatment without change of alkaline solution. The higher gel strength (298.7 g) was achieved using NaOH solution 3 M, 105 min and pre-treatment without change of the alkaline solution. As for the melting point, the higher value (29.1°C) was obtained with NaOH solution 4 M, 45 min, and pre-treatment with change of NaOH solution. To the bones extraction, the higher gelatin yield was reached with size 1 mm (4.86%). The higher gel strength (128.2 and 131.5 g) were not significantly difference, and they were found in the first extraction with bones size 1 and 2 mm, respectively. Using 2 mm of granulometry, it was possible to obtain the higher melting point values, being 28.5°C to the first extraction.
Sy, Dicken. "Characterization and purification of sex hormone binding globulin in the common carp (Cyprinus carpio) /." Hong Kong : University of Hong Kong, 1998. http://sunzi.lib.hku.hk/hkuto/record.jsp?B19470484.
Full textDaud, Hassan Bin Hj Mohd. "Experimentally induced infectious pancreatic necrosis (IPN) virus infection in common carp ('Cyprinus carpio', Linnaeus)." Thesis, Kingston University, 1989. http://eprints.kingston.ac.uk/20349/.
Full textAhmad, Tagried S. "The effect of non-steroid growth promotants on the growth of common carp." Thesis, Aston University, 1986. http://publications.aston.ac.uk/14501/.
Full text施德恒 and Dicken Sy. "Characterization and purification of sex hormone binding globulin in the common carp (Cyprinus carpio)." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1998. http://hub.hku.hk/bib/B31219901.
Full textPenne, Christopher Rhoades. "Radio telemetry study of common carp in Clear Lake, Iowa, to guide future management." [Ames, Iowa : Iowa State University], 2007.
Find full textMiest, Joanna Junack. "Apoptosis and its association with immunomodulation and disease in common carp (Cyprinus carpio L.)." Thesis, Keele University, 2013. http://eprints.keele.ac.uk/17/.
Full textCartwright, Jamie. "Isolation, purification and detection of C-reactive protein from the common carp Cyprinus carpio." Thesis, Keele University, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.401043.
Full textWilliams, Paul Edwin Hudak Paul F. "Evaluation of a common carp (Cyprinus carpio L.) exclusion and trapping device for use in aquatic plant founder colony establishment." [Denton, Tex.] : University of North Texas, 2008. http://digital.library.unt.edu/permalink/meta-dc-6038.
Full textBrown, Richard S. "Winter ecology of brown trout, white sucker and common carp in the Grand River, Ontario." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0027/NQ51182.pdf.
Full textMurakaeva, Asiya. "Structure, evolution and expression of the duplicated growth hormone genes of common carp (Cyprinus carpio)." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2009. http://dx.doi.org/10.18452/15982.
Full textThe common carp, Cyprinus carpio, is a tetraploid fish species from the family Cyprinidae that arose about 20-50 Myr ago. The aim of the present work was attempting to understand the functional role of the duplicated common carp GH genes by studying their structure, evolution and expression. The introns of the second GH gene of common carp were sequenced for the first time and sequence comparisons of coding and non-coding regions of alleles of both GH genes were carried out. A phylogenetic analysis was done to examine the relationships of common carp GH genes with GH genes of the tetraploid goldfish and other diploid Cyprinids. In addition, phylogenetic analyses were done with other duplicated genes of common carp, some of which also important for growth. The relative rate test of Tajima (1993) showed a statistically significant increase in the evolution rate of the common carp GH I gene. In addition, some other duplicated gene pairs in common carp and goldfish with relaxation of functional constraints or even evidence of positive Darwinian selection in one of the two gene duplicates were found in the present study. The test of expression rates of the two GH genes has shown that the GH I and GH II genes were expressed at similar levels in carp fry. In contrast, the expression of GH II was statistically significantly lower than that of GH I in one year old carp, three years old males and females as well as in 10 months old fish adapted to cold temperature (2°C). To enable testing the hypothesis if activity of GH diverged between different GH variants of common carp a new and simple method for production of recombinant, biologically active GH proteins without the necessity of refolding was developed.
Lupica, Samuel J. "Nitrate Toxicity to Common Carp Measured Noninvasively by Novel Enzyme-linked Immunosorbent Assay for Cortisol." University of Toledo Health Science Campus / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=mco1226956326.
Full textFrancis, George. "Effects of low dietary levels of saponins on two common culture fish - common carp (Cyprinus carpio L.) and Nile tilapia (Oreochromis niloticus (L.))." [S.l. : s.n.], 2001. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB10316339.
Full textLee, J. A. C. "Biochemical, biophysical and morphological studies of temperature acclimation in the intestine of the common carp (Cyprinus carpio, L.)." Thesis, University of Liverpool, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.382061.
Full textJafarpour, Khozaghi Seyed Ali, and ali jafarpour@rmit edu au. "Quality characteristics of common carp (Cyprinus carpio) Surimi and Kamaboko and the role of Sarcaoplasmic Proteins." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081216.144930.
Full textLee, R. S. "The development of Sanguinicola inermis Plehn. 1905 (Digenea : Sanguinicolidae) in the common carp (Cyprinus carpio L.)." Thesis, Royal Holloway, University of London, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.517743.
Full textBeach, Mark Andrew. "Experimental studies on the control and regulation of feeding in the common carp, Cyprinus carpio (L.)." Thesis, London Metropolitan University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315493.
Full textCols, Vidal Montserrat. "Cellular and molecular analysis on apoptosis in the immune cells of common carp (Cyprinus carpio L.)." Thesis, Keele University, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.436183.
Full textChakravarthy, Chitra. "Apoptosis in the immune system of the common carp (Cyprinus carpio) : a cellular and molecular approach." Thesis, Keele University, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.397483.
Full textMohan, C. V. "Modulatory effects of cadmium and copper on the susceptibility and immune response of common carp, Cyprinus carpio (L) to selected pathogens." Thesis, University of Stirling, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.280056.
Full textPionnier, Nicolas. "Immunomodulation of the innate response in common carp Cyprinus carpio by β-glucan feeding and pathogenic infection." Thesis, Keele University, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.699664.
Full textBrogden, Graham [Verfasser]. "Cell-pathogen interactions in common carp (Cyprinus carpio L.): Studies on cell membranes and neutrophil responses / Graham Brogden." Hannover : Bibliothek der Tierärztlichen Hochschule Hannover, 2013. http://d-nb.info/1046662090/34.
Full textSyakuri, Hamdan [Verfasser]. "Studies of intestinal barrier functions of common carp, Cyprinus carpio, under feeding modulation and pathogen challenge / Hamdan Syakuri." Hannover : Bibliothek der Tierärztlichen Hochschule Hannover, 2013. http://d-nb.info/1030453527/34.
Full textHossain, M. A. "Nutritional evaluation of some Bangladeshi oilseed by-products as dietary protein sources for common carp (Cyprinus carpio L)." Thesis, University of Stirling, 1988. http://hdl.handle.net/1893/1803.
Full textSteele, IV William B. "Tissue-specific Bioconcentration Factor of the Synthetic Steroid Hormone Medroxyprogesterone Acetate (Mpa) in the Common Carp, Cyprinus Carpia." Thesis, University of North Texas, 2013. https://digital.library.unt.edu/ark:/67531/metadc500141/.
Full textAhmed, Arafat R. "The effect of dietary chromium (III) on growth and carbohydrate utilization in mirror and common carp (Cyprinus carpio) L." Thesis, University of Plymouth, 2012. http://hdl.handle.net/10026.1/1091.
Full textChaimongkol, Atra Dunham Rex A. "Disruption of embryonic development in common carp, Cyprinus carpio, and channel catfish, Istalurus punctatus, via knock down of BMP2 gene for repressible transgenic sterilization." Auburn, Ala, 2009. http://hdl.handle.net/10415/1594.
Full textCrockford, Tony. "The effects of temperature acclimation on the expression of contractile protein isoforms in the skeletal muscle of the common carp (Cyprinus carpio)." Thesis, University of St Andrews, 1989. http://hdl.handle.net/10023/14940.
Full textKongchum, Pawapol. "Isolation of innate immune response genes, expression analysis, polymorphism identification and development of genetic markers for linkage analysis in common carp (Cyprinus carpio)." Diss., Virginia Tech, 2010. http://hdl.handle.net/10919/77300.
Full textPh. D.
Gilad, Oren. "Characterization and control of the koi herpesvirus (KHV), a newly recognized pathogen of koi (Cyprinus carpio koi) and common carp (Cyprinus carpio carpio) /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2003. http://uclibs.org/PID/11984.
Full textWinker, Henning. "Post-impoundment population dynamics of non-native common carp Cyprinus Carpio in relation to two large native cyprinids in Lake Gariep, South Africa." Thesis, Rhodes University, 2011. http://hdl.handle.net/10962/d1005156.
Full textMurakaeva, Asiya [Verfasser], G. A. [Gutachter] Brockmann, P. [Gutachter] Hammerstein, and R. [Gutachter] Tiedemann. "Structure, evolution and expression of the duplicated growth hormone genes of common carp (Cyprinus carpio) / Asiya Murakaeva ; Gutachter: G. A. Brockmann, P. Hammerstein, R. Tiedemann." Berlin : Humboldt-Universität zu Berlin, 2009. http://d-nb.info/1208076329/34.
Full textHULÁK, Martin. "Sex control of common carp (Cyprinus carpio L.)." Doctoral thesis, 2007. http://www.nusl.cz/ntk/nusl-85761.
Full textJeng, Juinn-ho, and 鄭俊和. "Expression of the common carp (Cyprinus carpio) Rhodopsin." Thesis, 1997. http://ndltd.ncl.edu.tw/handle/11054338718160377917.
Full text國立臺灣大學
漁業科學研究所
85
In order to understand the physiology of the fish vision, we constructed a plasmid, pET32-Rho, which encoded the coding region of rhodopsin cDNA and was driven by T7 promoter. The recombinant rhodopsin is a fusion protein with thioredoxin and 6 histidine residues at the amino terminus. After IPTG induction, the cell extracts of Escherichia coli BL21(DE3) containing pET32-Rho was collected and run through the Ni2+ affinity column chromatography, and then their proteins were analyzed by SDS- polyacrylamide gel electrophoresis. Results demonstrated that a band with molecular mass of 55 kD was shown on the gel, but no positive reaction for western blot analysis by using anti-bovine rhodopsin polyclonal antibody(CERN886). The coding region of rhodospin cDNA was inserted into the baculovirus transfer vector, pBAC-Rho, under the control of the polyhedrin promoter. Linearlized virus DNA and the construct plasmid were co-infected Sf9 cells. Cells infected by recombinant virus were screened, purified and amplified. Extracts of insect cells infected with the recombinant virus at MOI of 5 after 72 hours. postinfection we recollected and treated with histidine-bind column.. Three major bands of 58 kD, 40 kD, and 36 kD were shown on the gel. However ,they were all immunologically positive with the polyclonal antibody (CERN886) in which the 40 kD band was excepted as recombinant rhodopsin. Further confirmation study remains to be investigated.
"Cloning of pollutant inducible genes from common carp, cyprinus carpio." Chinese University of Hong Kong, 1996. http://library.cuhk.edu.hk/record=b5888789.
Full textThesis (M.Phil.)--Chinese University of Hong Kong, 1996.
Includes bibliographical references (leaves 153-177).
Acknowledgments --- p.i
Presentations Derived from the Present thesis Work --- p.ii
Abstract --- p.iii
Abbreviations --- p.v
Abbreviation Table for Amino Acids --- p.viii
List of Figures --- p.ix
List of Tables --- p.xi
Contents --- p.xii
Chapter 1 --- Introduction --- p.1
Chapter 1.1 --- Environmental Pollutants --- p.1
Chapter 1.2 --- Pollutant Inducible Genes (PIGs) --- p.1
Chapter 1.2.1 --- Classification of PIGS --- p.2
Chapter 1.2.1.1 --- Drug Metabolizing Enzymes/Proteins --- p.2
Chapter 1.2.1.2 --- Stress Proteins --- p.5
Chapter 1.2.1.3 --- Antioxidant Enzymes --- p.6
Chapter 1.2.1.4 --- "Hormones, Growth Factors and Their Receptors" --- p.6
Chapter 1.2.1.5 --- Enzymes/Proteins Involved in Bioenergetics --- p.6
Chapter 1.2.2 --- PIGs as a Field of Study --- p.8
Chapter 1.2.2.1 --- Study of the Mechanism of Detoxification and Toxication --- p.8
Chapter 1.2.2.2 --- Biomarker Study --- p.9
Chapter 1.2.2.3 --- Study of Regulation of Gene Expression --- p.11
Chapter 1.2.2.4 --- Study of Evolution --- p.12
Chapter 1.3 --- Aims and Rational of the Present Study --- p.12
Chapter 2 --- General Methodology --- p.15
Chapter 2.1 --- Materials --- p.15
Chapter 2.2.1 --- Reagents --- p.15
Chapter 2.1.1.1 --- Preparation of Plasmid DNA --- p.15
Chapter 2.1.1.2 --- Preparation of Genomic DNA --- p.15
Chapter 2.1.1.3 --- Purification of Total RNA --- p.16
Chapter 2.1.1.4 --- Restriction Enzyme Digestion --- p.16
Chapter 2.1.1.5 --- Capillary Blotting of DNA (Southern Blotting) --- p.16
Chapter 2.1.1.6 --- Capillary Blotting of Total RNA (Northern Blotting) --- p.17
Chapter 2.1.1.7 --- Hybridization --- p.17
Chapter 2.1.1.8 --- Library Screening --- p.18
Chapter 2.1.1.9 --- Polymerase Chain Reaction --- p.18
Chapter 2.1.1.10 --- Transformation of E. coli Competent Cells --- p.19
Chapter 2.1.1.11 --- Nucleotide Sequence Determination --- p.19
Chapter 2.1.2 --- List of Primers --- p.20
Chapter 2.1.2.1 --- Primers used for Nucleotide Sequence Determination --- p.20
Chapter 2.1.2.2 --- Primer Used for First Strand cDNA Synthesis --- p.20
Chapter 2.1.2.3 --- Primers for Amplifying Actin cDNA Fragment --- p.20
Chapter 2.1.2.4 --- Common Carp MT Specific Primers --- p.20
Chapter 2.1.2.5 --- Teleost CYP1A Specific Primers --- p.21
Chapter 2.1.2.6 --- Common Carp CYP1A Specific Primers --- p.21
Chapter 2.1.2.7 --- Primers and Cassettes for the Cloning of5' Upstream Regions of MT Genes --- p.21
Chapter 2.1.3 --- Accession Numbers of Selected P450 and MT Nucleotide and Amino Acid Sequences in the Genebank --- p.21
Chapter 2.1.3.1 --- MTs of Different Teleost Species --- p.21
Chapter 2.1.3.2 --- MTs of Other Vertebrate Species' --- p.22
Chapter 2.1.3.3 --- P450s of Different Teleost Species --- p.22
Chapter 2.1.3.4 --- CYP1s of Different Mammalian Species --- p.22
Chapter 2.2 --- Methods --- p.23
Chapter 2.2.1 --- Preparation of Plasmid --- p.23
Chapter 2.2.2 --- Preparation of Genomic DNA --- p.23
Chapter 2.2.3 --- Purification of Total RNA --- p.24
Chapter 2.2.4 --- Restriction Enzyme Digestion --- p.25
Chapter 2.2.5 --- Capillary Blotting of DNA (Southern Blotting) --- p.25
Chapter 2.2.5.1 --- Semi-dry Capillary Blotting --- p.25
Chapter 2.2.5.2 --- Alkaline Transfer --- p.25
Chapter 2.2.5.3 --- Transfer of Digested Genomic DNA on to Nylon Membrane --- p.26
Chapter 2.2.6 --- Capillary Blotting of Total RNA (Northern Blotting) --- p.26
Chapter 2.2.7 --- Radioactive Labeling of Nucleic Acid Probes --- p.26
Chapter 2.2.8 --- Hybridization --- p.27
Chapter 2.2.9 --- Library Screening --- p.27
Chapter 2.2.9.1 --- Construction of Liver cDNA Library of Adult Common Carp --- p.27
Chapter 2.2.9.2 --- Preparation of Plating Cells --- p.27
Chapter 2.2.9.3 --- Phage Tittering --- p.27
Chapter 2.2.9.4 --- Primary Screening --- p.28
Chapter 2.2.9.5 --- Secondary Screening
Chapter 2.2.9.6 --- Conversion of Phage DNA to Phagemid by invivo Excision --- p.28
Chapter 2.2.10 --- First Strand cDNA Synthesis --- p.29
Chapter 2.2.11 --- Polymerase Chain Reaction --- p.29
Chapter 2.2.12 --- Ligation of DNA with Linearized Plasmid --- p.30
Chapter 2.2.13 --- Transformation of E. coli Competent Cell --- p.30
Chapter 2.2.14 --- Nucleotide Sequence Determination --- p.31
Chapter 2.2.15 --- Densitometric Analysis --- p.31
Chapter 3 --- "Cloning of Common Carp MT cDNA and Gene, and Induction of MT mRNA Expression" --- p.32
Chapter 3.1 --- Introduction --- p.32
Chapter 3.1.1 --- Metals in Biological System --- p.32
Chapter 3.1.2 --- Metallothionein --- p.33
Chapter 3.1.2.1 --- Functions of MT --- p.26
Chapter 3.1.2.2 --- Regulation of MT Expression --- p.39
Chapter 3.1.3 --- Fish MTs --- p.44
Chapter 3.1.3.1 --- Detection of MT in Teleost --- p.46
Chapter 3.1.3.2 --- MT Studies in Common Carp --- p.47
Chapter 3.1.4 --- Specific Aims of This Chapter --- p.49
Chapter 3.2 --- Strategies --- p.50
Chapter 3.3 --- Specific Methods --- p.50
Chapter 3.3.1 --- Cloning of MT cDNAs of Common Carp --- p.50
Chapter 3.3.2 --- Analysis of MT cDNA Sequences --- p.51
Chapter 3.3.3 --- Southern Blot Analysis of Common Carp Genomic DNA --- p.52
Chapter 3.3.4 --- Amplification of MT Gene Fragments Using PCR --- p.52
Chapter 3.3.5 --- Amplification of the 5' Upstream Regions of MT Genes Using PCR --- p.52
Chapter 3.3.6 --- Endogenous MT mRNA Expression of Juvenile and Adult Common Carp --- p.54
Chapter 3.3.7 --- Induction of MT mRNA of Juvenile Common Carp Injected with Cadmium --- p.55
Chapter 3.4 --- Results --- p.56
Chapter 3.4.1 --- Cloning of Common Carp MT cDNAs --- p.56
Chapter 3.4.2 --- Analysis of the MT cDNA Sequences --- p.57
Chapter 3.4.3 --- Southern Blot Analysis of the Common Carp Genomic DNA --- p.59
Chapter 3.4.4 --- Amplification of the MT Gene Fragments of Common Carp Using PCR --- p.62
Chapter 3.4.5 --- Amplification of the 5' Upstream Regions of MT Genes using PCR --- p.65
Chapter 3.4.6 --- Endogenous MT mRNA Expression of Juvenile and Adult Common Carp --- p.67
Chapter 3.4.7 --- Induction of MT mRNA of Juvenile Common Carp Injected with Cadmium --- p.68
Chapter 3.5 --- Discussion --- p.72
Chapter 3.5.1 --- MT cDNAs of Common Carp --- p.72
Chapter 3.5.1.1 --- Coding Region --- p.72
Chapter 3.5.1.2 --- The 3' Untranslated Region --- p.75
Chapter 3.5.1.3 --- The 5' Untranslated Region --- p.76
Chapter 3.5.2 --- MT Genes of Common Carp --- p.77
Chapter 3.5.3 --- MT mRNA Expression of Common Carp --- p.82
Chapter 3.5.4 --- Normalization of the Signals of Northern Blot Analysis --- p.85
Chapter 3.5.5 --- Common Carp MT mRNA as Biomarker of Heavy Metal Exposure? --- p.87
Chapter 3.6 --- Conclusion --- p.89
Chapter 4 --- Cloning of Common Carp CYP1A cDNAs and Induction of CYP1A mRNA Expression --- p.90
Chapter 4.1 --- Introduction --- p.90
Chapter 4.1.1 --- Cytochrome P450s --- p.90
Chapter 4.1.2 --- Cytochrome P450 1 (CYP1) --- p.93
Chapter 4.1.3 --- AhR Mediated CYP1A1 Gene Induction --- p.94
Chapter 4.1.3.1 --- Anthropogenic Sources of AhR Ligands --- p.95
Chapter 4.1.3.2 --- Natural Sources of AhR Ligands --- p.97
Chapter 4.1.3.3 --- Potency of Inducibility --- p.97
Chapter 4.1.3.4 --- Induction of CYP1A1 Gene Transcription by AhR --- p.98
Chapter 4.1.3.5 --- Non-AhR Mediated CYP1A1 Gene Transcription? --- p.105
Chapter 4.1.4 --- CYP1A Studies in Teleost Species --- p.107
Chapter 4.1.4.1 --- Regulation of CYP1A in Teleost --- p.109
Chapter 4.1.4.2 --- Detection of CYP1A in Teleost --- p.111
Chapter 4.1.4.3 --- CYP1A Studies of Common Carp --- p.113
Chapter 4.1.5 --- Specific Aims of This Chapter --- p.114
Chapter 4.2 --- Strategies --- p.115
Chapter 4.3 --- Specific Methods --- p.119
Chapter 4.3.1 --- RT-PCR of CYP1A cDNAs of Common Carp --- p.119
Chapter 4.3.2 --- Determination of the Nucleotide Sequences of the CYP1A cDNAs of Common Carp --- p.119
Chapter 4.3.3 --- Library Screening --- p.119
Chapter 4.3.4 --- Analysis of the CYP1A Genes of Common Carp --- p.121
Chapter 4.3.5 --- Induction of CYP1A mRNA of Common Carp Injected with 3-MC --- p.122
Chapter 4.4 --- Results --- p.123
Chapter 4.4.1 --- RT-PCR of CYP1A cDNAs of Common Carp --- p.123
Chapter 4.4.2 --- Determination of the Nucleotide Sequences of the CYP1A cDNAs of Common Carp --- p.124
Chapter 4.4.3 --- Library Screening --- p.124
Chapter 4.4.4 --- Analysis of the CYP1A Genes of Common Carp --- p.128
Chapter 4.4.5 --- Induction of CYP1A mRNA of Common Carp Injected with 3-MC --- p.131
Chapter 4.5 --- Discussion --- p.134
Chapter 4.5.1 --- On the Use of Rainbow Trout CYP1A1 cDNA Probe --- p.134
Chapter 4.5.2 --- CYP1A cDNAs of Common Carp --- p.134
Chapter 4.5.3 --- CYP1A Genes of Common Carp --- p.138
Chapter 4.5.4 --- CYP1A Expression in Uninduced and Induced Tissues --- p.142
Chapter 4.5.5 --- The Use of CYP1A cDNAs As Biomarkers --- p.146
Chapter 4.6 --- Conclusion --- p.148
Chapter 5 --- General Conclusion --- p.149
Chapter 6 --- References --- p.153
Huang, Yun-Cheih, and 黃韻潔. "Studies on Distribution of the 43 kDa Zn-Binding Protein in Common Carp, Grass Carp, Silver Carp and Tilapia by Using Immunoassay." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/14620432929980057945.
Full text國立臺灣海洋大學
食品科學系
94
Abstract Common carp always has high concentration of zinc in its digestive tract tissue which mainly comes from a 43 kDa zinc-binding protein. Detergent (lubrol) was used to extract this 43 kDa zinc-binding protein from living organism. Lubrol only could extract 5% of the zinc-binding protein from nuclei/cell debris fraction of digestive tract tissue of common carp. Adding 4 M guanidine hydrochloride to the lubrol increased the extraction ratio to 85%. Zn2+-IMAC and SDS-PAGE analysis indicated that the major protein in the guanidine/lubrol extract was the 43 kDa zinc-binding protein. In immunoassay, the guanidine/lubrol extracts reacted with the antibody against 43 kDa zinc-binding protein dose dependently. A standard calibration curve of the guanidine hydrochloride/lubrol extract against the immuno-response was obtained. The standard calibration curve was used to examine whether the 43 kDa zinc-binding protein exist in the guanidine hydrochloride/lubrol extract of other fishes. It was found that the 43 kDa Zinc-binding protein both exist in common carp’s kidney and spleen. The 43 kDa zinc-binding protein also existed in the digestive tract tissue and spleen of grass carp and silver carp which are the same families of Cyprinidae. However, the protein does not exist in the muscle of common carp, grass carp and silver carp. In tilapia, the species and genus are far from common carp, in all tissue tilapia no immuno-response against the antibody of 43 kDa zinc-binding protein was found. Existence of the 43 kDa zinc-binding protein in animal tissue seems to be related to organisms’ species and genus.
"ONTOGENETIC AND MORPHOLOGICAL EFFECTS OF PERSONALITY IN COMMON CARP (CYPRINUS CARPIO)." Thesis, 2013. http://hdl.handle.net/10388/ETD-2013-08-1179.
Full text"Characterization of common carp (cyprinus carpio) insulin-like growth factor genes." 1997. http://library.cuhk.edu.hk/record=b5895734.
Full textThesis (M.Phil.)--Chinese University of Hong Kong, 1997.
Includes bibliographical references (leaves 112-120).
ACKNOWLEDGMENTS --- p.i
ABSTRACT --- p.ii
TABLE OF CONTENTS --- p.iii
Chapter CHAPTER 1 --- INTORDUCTION --- p.1
Chapter 1.1 --- General Introduction --- p.1
Chapter 1.2 --- Historical Overview --- p.3
Chapter 1.2.1 --- Insulin-Like Growth Factors I and II --- p.3
Chapter 1.2.2 --- IGF Receptors --- p.5
Chapter 1.2.3 --- IGF Binding Proteins --- p.7
Chapter 1.3 --- Origin and Production of IGFs --- p.7
Chapter 1.3.1 --- The Hypothalamo-Pituitary-GH-IGF-I Axis --- p.7
Chapter 1.3.2 --- Factors Regulating IGF production --- p.9
Chapter 1.3.3 --- Expression of IGFs in the Central Nervous System --- p.11
Chapter 1.4 --- Actions of IGFs --- p.12
Chapter 1.4.1 --- Insulin-like Metabolic Effects --- p.12
Chapter 1.4.2 --- Mitogenic Effects --- p.13
Chapter 1.4.3 --- Effects on Differentiation --- p.13
Chapter 1.4.4 --- IGFs in Reproductive System --- p.14
Chapter 1.4.5 --- IGF Actions in the Central Nervous System --- p.14
Chapter 1.5 --- Transgenic and Knockout Animal Models for IGFs --- p.15
Chapter 1.6 --- Molecular Biology of IGFs --- p.17
Chapter 1.6.1 --- Structure of the IGF Genes --- p.17
Chapter 1.6.2 --- Expression of IGF Genes --- p.21
Chapter 1.6.3 --- Regulation of IGF Gene Expression --- p.23
Chapter 1.7 --- IGF Receptors --- p.24
Chapter 1.7.1 --- IGF-I Receptor --- p.24
Chapter 1.7.2 --- IGF-II Receptor --- p.26
Chapter 1.8 --- IGFBPs --- p.26
Chapter 1.9 --- Teleost IGFs --- p.28
Chapter 1.9.1 --- The GH-IGF-Axis in Teleost --- p.28
Chapter 1.9.2 --- Osmoregulation and Other Biological Actions of IGFin Teleost --- p.29
Chapter 1.9.3 --- Molecular Biology of IGFs in Teleost --- p.30
Chapter 1.9.4 --- IGFBPs and IGF Receptors in Teleost --- p.31
Chapter 1.10 --- Rationale and Aim of the Present Study --- p.32
Chapter CHAPTER 2 --- SEARCH OF IGF-I PROMOTER BY GENOMIC DNA POLYMERASE CHAIN REACTION --- p.34
Chapter 2.1 --- Introduction --- p.34
Chapter 2.2 --- Materials --- p.35
Chapter 2.3 --- Methods --- p.39
Chapter 2.3.1 --- Preparation of Genomic DNA from Carp Testis --- p.39
Chapter 2.3.2 --- Restriction Enzyme Digestion of Genomic DNA --- p.40
Chapter 2.3.3 --- Polymerase Chain Reaction --- p.40
Chapter 2.3.3.1 --- Ligation of the Cassette to Digested Genomic DNA --- p.40
Chapter 2.3.3.2 --- Amplification by PCR --- p.40
Chapter 2.3.4 --- Agarose Gel Electrophoresis --- p.42
Chapter 2.3.5 --- Gene Clean Using Sephaglas´ёØ BandPrep Kit (Pharamica) --- p.42
Chapter 2.3.6 --- Cloning of PCR Products --- p.43
Chapter 2.3.7 --- Transformation of Competent Cell (Heat Shock Method) --- p.43
Chapter 2.3.8 --- Small Scale Alkaline Preparation of Plasmid DNA --- p.44
Chapter 2.3.9 --- Restriction Enzyme Digestion to Release the Insert --- p.45
Chapter 2.3.10 --- Large Scale Plasmid Preparation of the Positive Clone --- p.45
Chapter 2.3.11 --- DNA Sequencing of the Positive Clone Using the T7 DNA Polymerase Sequencing Kit (Pharmacia) --- p.46
Chapter 2.4 --- Results and Discussion --- p.49
Chapter CHAPTER 3 --- ISOLATION OF GENOMIC CLONES CARRYING THE IGF-I GENE --- p.55
Chapter 3.1 --- Introduction --- p.55
Chapter 3.2 --- Materials --- p.56
Chapter 3.3 --- Methods --- p.58
Chapter 3.3.1 --- Preparation of the Plating Host Cells --- p.58
Chapter 3.3.2 --- Phage Titering --- p.58
Chapter 3.3.3 --- Primary Screening of Common Carp Genomic Library --- p.59
Chapter 3.3.4 --- Preparation of Radioactive Nucleic Acid Probes --- p.60
Chapter 3.3.5 --- Purification of the Positive Clones --- p.60
Chapter 3.3.6 --- Purification of DNA from Lambda Phage Using Sephaglas´ёØ PhagePrep Kit (Pharmacia) --- p.61
Chapter 3.3.7 --- Restriction Enzyme Digestion Release of Inserts --- p.62
Chapter 3.3.8 --- Capillary Transfer of DNA to Nylon Membrane Under Alkaline Condition --- p.62
Chapter 3.3.9 --- Southern Analysis of the 10 Positive Clones --- p.63
Chapter 3.3.10 --- Restriction Mapping of the Clone P1 --- p.64
Chapter 3.3.11 --- Subcloning of the Fragments of the Clone PI into Plasmid Vector --- p.64
Chapter 3.3.12 --- IGF-I Specific PCR --- p.64
Chapter 3.3.13 --- Amplification of Introns from the Clone P1 Using PCR --- p.67
Chapter 3.4 --- Results and Discussion --- p.70
Chapter CHAPTER 4 --- RNA ASSAY USING REVERSE TRANSCRIPTION- POLYMERASE CHAIN REACTION --- p.83
Chapter 4.1 --- Introduction --- p.83
Chapter 4.2 --- Materials --- p.85
Chapter 4.3 --- Methods --- p.86
Chapter 4.3.1 --- Administration of Hormones --- p.86
Chapter 4.3.1.1 --- Injection Time Course1 --- p.86
Chapter 4.3.1.2 --- Injection Time Course2 --- p.86
Chapter 4.3.2 --- Total RNA Extraction --- p.87
Chapter 4.3.2.1 --- Rapid RNA Isolation --- p.87
Chapter 4.3.3 --- Electrophoresis of RNA in Agarose Gel Containing Formaldehyde --- p.88
Chapter 4.3.4 --- Rapid Isolation of PolyA+ mRNA from Total RNA --- p.89
Chapter 4.3.5 --- IGF-I Specific RT-PCR --- p.90
Chapter 4.4 --- Results and Discussion --- p.92
Chapter CHAPTER 5 --- SEARCH FOR IGF-II GENE USING GENOMIC SOUTHERN BLOT ANALYSIS --- p.101
Chapter 5.1 --- Introduction --- p.101
Chapter 5.2 --- Materials --- p.103
Chapter 5.3 --- Methods --- p.104
Chapter 5.3.1 --- Preparation of Genomic DNA from Carp Testis --- p.104
Chapter 5.3.2 --- Restriction Enzyme Digestion of Genomic DNA --- p.104
Chapter 5.3.3 --- Southern Blotting of the Digested Genomic DNA --- p.104
Chapter 5.3.4 --- Preparation of the Trout IGF-II Specific Probe --- p.104
Chapter 5.3.5 --- Genomic Southern Hybridization --- p.105
Chapter 5.4 --- Results and Discussion --- p.106
Chapter CHAPTER 6 --- GENERAL DISCUSSION AND CONCLUSION --- p.109
REFERENCES --- p.112
"Common carp (cyprinus carpio) IGF-II: molecular cloning and expression studies." 2001. http://library.cuhk.edu.hk/record=b5890718.
Full textThesis (M.Phil.)--Chinese University of Hong Kong, 2001.
Includes bibliographical references (leaves 130-146).
Abstracts in English and Chinese.
Acknowledgments --- p.i
Abstract --- p.ii
論文撮要 --- p.iii
List of Figures and Tables --- p.iv
Abbreviations --- p.vi
Table of contents --- p.vii
Chapter Chapter I --- Introduction --- p.1
Chapter 1.1 --- Literature review --- p.1
Chapter 1.1.1 --- An overview of IGFs --- p.3
Chapter 1.1.2 --- Molecular biology of IGFs --- p.5
Chapter 1.1.2.1 --- IGF-I and IGF-II genes and mRNAs --- p.5
Chapter 1.1.2.2 --- Amino acid sequences of IGF-II --- p.8
Chapter 1.1.2.3 --- Imprinting of IGF-II --- p.12
Chapter 1.1.3 --- IGF distribution in tissues and body fluids --- p.14
Chapter 1.1.3.1 --- IGF in serum --- p.14
Chapter 1.1.3.2 --- IGF binding proteins --- p.16
Chapter 1.1.4 --- IGF receptors --- p.19
Chapter 1.1.4.1 --- Structures of the IGF receptors --- p.20
Chapter 1.1.4.2 --- Ligand binding of the IGF receptors --- p.21
Chapter 1.1.4.3 --- Signal transduction and biological response --- p.22
Chapter 1.1.5 --- Biological effects of IGF --- p.24
Chapter 1.1.6 --- Expression of recombinant IGF --- p.28
Chapter 1.2 --- Rationale and Objective --- p.29
Chapter Chapter II --- Methodology --- p.33
Chapter 2.1 --- Design of degenerate primers --- p.33
Chapter 2.2 --- Cloning --- p.35
Chapter 2.2.1 --- DNA extraction from agarose gel --- p.35
Chapter 2.2.2 --- Linearization and dephosphorylation of plasmid DNA --- p.35
Chapter 2.2.3 --- Blunt-end ligation of amplicon with linearized plasmid --- p.36
Chapter 2.2.4 --- T/A ligation of amplicon with linearized plasmid --- p.37
Chapter 2.2.5 --- Sticky end ligation of foreign DNA with linearized plasmid --- p.37
Chapter 2.2.6 --- Preparation of competent of E. coli stain DHI5α cells --- p.38
Chapter 2.2.7 --- Transformation of plasmid vector into competent cells (heat-shock/ electroporation) --- p.39
Chapter 2.2.8 --- "Spread single colony, PCR check clone and inoculation" --- p.40
Chapter 2.2.9 --- Small scale alkali preparation of plasmid DNA --- p.41
Chapter 2.2.10 --- Large scale preparation of plasmid DNA --- p.41
Chapter 2.2.11 --- Nucleotide sequencing --- p.41
Chapter 2.2.11.1 --- Manual sequencing --- p.41
Chapter 2.2.11.2 --- PCR sequencing --- p.43
Chapter 2.3 --- Northern blot --- p.45
Chapter 2.4 --- Preparation of radio-labeled probe and hybridization of radio-labeled probe to nylon immobilized nucleic acid --- p.46
Chapter 2.5 --- RACE --- p.48
Chapter 2.5.1 --- Design of gene-specific primer --- p.51
Chapter 2.5.2 --- First strand cDNA synthesis --- p.51
Chapter 2.5.3 --- TdT tailing of cDNA --- p.52
Chapter 2.6 --- Poly-A tract extraction --- p.53
Chapter 2.7 --- Tissue distribution of mRNA --- p.53
Chapter 2.7.1 --- Tissue preparation --- p.53
Chapter 2.7.2 --- Total RNA extraction --- p.54
Chapter 2.7.3 --- Formaldehyde agarose gel electrophoresis of RNA --- p.54
Chapter 2.8 --- RNAse protection assay --- p.55
Chapter 2.8.1 --- Antisense probe generation --- p.56
Chapter 2.8.2 --- Preparation of the sample RNA --- p.58
Chapter 2.8.3 --- Hybridization --- p.58
Chapter 2.8.4 --- RNase digestion of hybridized probe and sample RNA --- p.59
Chapter 2.8.5 --- Preparation of radioactive marker --- p.60
Chapter 2.8.6 --- Separation and detection of protected fragments --- p.60
Chapter 2.8.7 --- Data processing and statistical analysis --- p.61
Chapter 2.9 --- Injection of GH --- p.62
Chapter 2.10 --- Recombinant protein expression --- p.62
Chapter 2.10.1 --- Plasmid construction --- p.62
Chapter 2.10.2 --- Expression --- p.63
Chapter 2.11 --- Resolution of proteins on SDS-PAGE --- p.63
Chapter 2.12 --- Purification --- p.64
Chapter 2.13 --- Western transfer --- p.64
Chapter 2.14 --- Immunodetection --- p.65
Chapter Chapter III --- Results & Discussion --- p.67
Chapter 3.1 --- Isolation and characterization of IGF-II cDNA and its gene organization --- p.67
Chapter 3.1.1 --- Introduction --- p.67
Chapter 3.1.2 --- Results --- p.68
Chapter 3.1.2.1 --- Generation of a fragment of the common carp IGF-II cDNA by PCR --- p.68
Chapter 3.1.2.2 --- Isolation of the full length common carp IGF-II cDNA by RACE. --- p.69
Chapter 3.1.2.3 --- Nucleotide sequence analysis --- p.74
Chapter 3.1.2.4 --- Relationship of common carp IGF-II to common carp IGF-I and insulin --- p.78
Chapter 3.1.2.5 --- Confirmation of the presence of IGF-II in common carp --- p.79
Chapter 3.1.2.6 --- Multiple mRNA forms of common carp IGF-I and IGF-II --- p.80
Chapter 3.1.2.7 --- Gene organization of the common carp IGF-II gene --- p.83
Chapter 3.1.3 --- Discussion --- p.86
Chapter 3.2 --- Tissue specific distribution of IGF-I and IGF-II mRNA and their hormonal regulation --- p.90
Chapter 3.2.1 --- Introduction --- p.90
Chapter 3.2.2 --- Results --- p.94
Chapter 3.2.2.1 --- RNase protection assay measurement of tissue mRNA levels in juvenile and adult common carp --- p.94
Chapter 3.2.2.2 --- Expression of IGF-II mRNA during larval development --- p.99
Chapter 3.2.2.3 --- Effect of GH on IGF-I and IGF-II mRNA levels in brain and Hver of juvenile common carp --- p.102
Chapter 3.2.3 --- Discussion --- p.106
Chapter 3.3 --- Recombinant common carp IGF-II expressed in E. coli --- p.110
Chapter 3.3.1 --- Introduction --- p.110
Chapter 3.3.2 --- Results --- p.112
Chapter 3.3.2.1 --- Product of recombinant common carp IGF-II --- p.112
Chapter 3.3.2.2 --- Purification of common carp IGF-II --- p.115
Chapter 3.3.2.3 --- Immunodetection --- p.117
Chapter 3.3.3 --- Discussion --- p.118
Chapter Chapter IV --- General conclusion --- p.120
Appendix: Reagents --- p.124
Reference list --- p.130
Yang, Jen-Lee, and 楊仁理. "Toxic effects of semiconductor metal gallium on common carp (Cyprinus carpio)." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/92255453647507538376.
Full text國立臺灣大學
動物學研究所
91
Gallium (Ga) is one of the intermetallic elements that are increasingly being used in making high-speed semiconductors. III-V compound semiconductors, such as GaAs and InGaAs, are important materials in the manufacture of optoelectronic devices and integrated circuits in the semiconductor industry. The research on gallium compound for use in semiconductors had been accompanied by an increasing amount of toxic materials released as potential toxic wastes, which were harmful to health and environment. The purpose of this study was to investigate the adverse effects of gallium concentrations on common carp (Cyprinus caripo L.). Median lethal concentrations (LC50) of gallium for fry (4 weeks old, 0.202 ± 0.006 g in body weight) and juvenile (12 weeks old, 2.3 ± 0.19 g in body weight) carp were obtained. LC50 value of fry carp at 96-h exposure was 12.55 mg/L, and LC50 value of juvenile carp was 19.78 mg/L after same exposure duration. Based on above datum, fry carp were exposed to sublethal levels of gallium (1.0, 2.0, 4.0 mg L-1) in a four-week testing period, and the effects on the growth rate were assessed. Decreasing growth rates were observed at the two highest exposure concentrations. At a gallium concentration of 1.0 mg/L, no inhibition of growth was observed in the present study. Juvenile carp were exposed for two weeks at 2.0, 4.0, and 8.0 Ga mg L-1. Changes in gills Induced hyperplasia of epithelial cells, subepithelial edema, and fusion of secondary lamellae in treated fish. Pathological alternations of the kidney were frequently found in tubular epithelia. These lesions appeared with increased severity at higher gallium levels. Juvenile carp were exposed to three different sublethal levels of gallium (2.0, 4.0, and 8.0 mg L-1) in chronic toxicity tests. During a 28-day testing period, serum metabolic enzyme activity (aspartate aminotransferase (AST), alanin aminotransferase (ALT), and alkaline phosphatase (ALP) was analyzed every 14 days. An increase of enzyme activity in serum was observed, particularly at the two highest exposure concentrations. Furthermore, it was found that means of the measured serum biochemistry parameters (including glucose, blood urea nitrogen, creatinine, cholesterol, and triglyceride) of these exposed groups significantly differed from those of the untreated group (p < 0.05). And, deformation of erythrocytes according to the peripheral blood smears examination at higher exposure levels (4.0 and 8.0 mg Ga L-1). Electron microscopy investigations revealed ultrastructural alterations in hepatocytes which were correlated with exposure concentrations and exposure time. Cytopathological effects included nuclei with irregular outlines and heterochromatin, fragmentation and vesiculation of endoplasmic reticulum, and disruption of mitochondria. Moreover, proliferation of lysosomes with electron-dense bodies and lipid inclusions were also found in the cytoplasm of hepatocytes. Apoptotic lymphocytes of juvenile carp spleen were identified and quantified by light microscopic in situ nick end labeling, electron microscopy, DNA gel electrophoresis, and apoptotic lymphocytes counting. Apoptotic lymphocytes increased in number at 12 h (5.5%) and peaked at 24h (13.2%) after the gallium injection. Terminal deoxynucleotidyl transferase mediated dUTP nick end-labeling staining for labeling of DNA fragmentation showed apoptotic lymphocytes were located on the margin of spleen neighboring epithelium. Apoptotic cells were phagocytosed by macrophages under electron microscopic observation. And ladders were found after 24h administration of gallium. Because the common carp is an important cultured fish species in fishponds near semiconductor manufacturing districts in Taiwan, it is a suitable model species to study the toxicity of semiconductor-related metals. And many wastewater discharges contain a mixture of pollutants, the combined effect of gallium with copper or zinc has to be carried out. The purposes of this study were to investigate the toxic effects of sublethal gallium concentrations on common carp. All of these findings support gallium being a potential pollutant, although no adverse effects following industrial exposure have been reported to date. However, the present results will provide information which can be used to objectively institute measures to minimize the pollution by gallium and its impacts on aquatic ecosystems.
Lo, Jung-Yu, and 羅榮煜. "Distribution and accumulation of the zinc in hematopoietic tissues of common carp." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/86918625018149247901.
Full text國立臺灣海洋大學
食品科學系
98
In order to know the zinc concentration in the hematopoietic tissues (head kidney, kidney and spleen) of the common carp, we respectively analyze the common carp from fish market (stressed fish) and from the laboratory (rested fish). The zinc concentration in the blood, head kidney, kidney and spleen of grass carp, silver carp and tilapia were also studied for a comparison. Zinc concentration in the blood of the common carp from fish market is 18.1±16.9 μg/ml whole blood, with a great individual difference. The zinc concentration in the head kidney, kidney and spleen of the common carp from fish market are 665±547,268±227 and 204±260 μg/g fresh tissue, respectively. The head kidney, kidney and spleen of the grass carp, silver carp and tilapia are between 10-20 μg/g fresh tissue with little individual difference among different species and different tissues. However, the zinc concentration in the blood, head kidney, kidney and spleen of common carp (stressed fish) are significantly higher than that of the laboratory (rested fish), and the main differences between the two groups are the zinc in the cells. The experiment also indicates that when the common carp were fed high zinc diet, the zinc will accumulate in the hematopoietic tissue (head kidney, kidney and spleen).
Fang, Szu-Wei, and 方思幃. "Proliferation of the hematopoietic cells in common carp head kidney under stress." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/84952913948457436199.
Full text國立臺灣海洋大學
食品科學系
100
The cell and zinc levels in the blood of stressed carp are higher than those of resting carp, at the same time, the cell and zinc levels in head kidney of stressed carp are also higher than those of resting carp. Head kidney is the hematopoietic organ of common carp, the increases of cell level in the blood under stress, may be produced by head kidney. In order to understand how the cells in head kidney of carp proliferate, and the relationship between proliferation and zinc, market carp (stressed carp) and laboratory carp (resting carp) were used as materials. The cells in head kidney of 15 resting carps and 14 stressed carps were separated by Percoll density into 2 layers, layer 1 (ρ = 1.02) and 2 (ρ = 1.07), respectively, and the cell levels in different layers were measured. It was found that the cell levels in layer 1 of stressed carp is significantly higher than those in resting carp, being 532x106 cells/g tissue to 118x106 cells/g tissue. The cell levels in layer 2 were 746x106 cells/g tissue to 776x106 cells/g tissue, respectively, there is no significant difference between the stressed and resting carp. In layer 1, the main proliferated cells had a cell size of ~ 6 μm, for the stressed carp being 354x106 cells/g tissue, and for resting carp being 86x106 cells/g tissue, the difference was 4 times. In light-microscopic observation of the Giemsa stain, most of the cells in layer 1 were round in size about 6 μm. They have thin layer cytoplasm and a round nucleus, it is very similar to hematopoietic stem cell/progenitor. The immunofluorescent stain with an antibody against the 43-kDa zinc-binding protein indicates there is more immunofluorescent response in the cells in layer 1 of the stressed carp. Ther results of staining with o-Dianisidine indicate there are more RBC in layer 2 of stressed carp. The cells of common carp head kidney were serial subcultured with 4 types of medium: medium (DMEM/F12) only, medium + 10 % carp serum, medium + 10 % carp serum + 0.3mM ZnCl2, and medium + 0.3mM ZnCl2. At different time intervals, the cultured cells were separated into 2 layers by Percoll density, layer 1 (ρ = 1.02) and layer 2 (ρ = 1.07), respectivey; and the cell level was measured. It was found that the group of medium + 10% carp serum + 0.3mM ZnCl2 has the best growth. Zinc induced the cells in carp head kidney to proliferate, but needed the supplementation of carp serum. In order to know the growth curve of the cell of carp head kidney under supplementation with or without zinc, the cells of carp head kidney were cultured with carp serum and zinc or carp serum only from h0 to h96. The cultured cells were then separated by Percoll density. The results indicate the cell levels in the group supplemented with carp serum and zinc of layer 1 at h0 was 3.60x106 cells/ml and at h96, 12.5 x106 cells/ml. The population doubling time of cells in layer 1 supplementaed carp serum and zinc was only 6 h, compared to that supplemented with serum only being 19 h. The layer 1 cells after being cultured for 3 days with zinc and carp serum were staind with an antibody against the 43-kDa zinc-binding protein. The results indicate that the 6 μm cells have immunofluorescent response. Besides, there are more RBC cells in layer 2. Zinc not only induce layer 1 cells to proliferate, but may also promote cell to differentiate to RBC. When carps are under stress, zinc is released from its digestive tract tissue to blood, then transported to head kidney. Zinc is possibly bound to transferrin in blood. In the head kidney, zinc-transferrin complex may be bound to transferrin receptor on hematopoietic stem cell/progenitor cells of the head kidney. This may further the cells proliferate to become RBC to help the carps to overcome stress.