Relevant bibliographies by topics / Bovine lactoferrin

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Bovine lactoferrin'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Bovine lactoferrin"

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Oria, Rosa, Maznah Ismail, Lourdes Sánchez, Miguel Calvo, and Jeremy H. Brock. "Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes." Journal of Dairy Research 60, no. 3 (August 1993): 363–69. http://dx.doi.org/10.1017/s0022029900027709.

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SummaryThe interaction of lactoferrin from human and bovine milk with the human promonocytic cell line U937 has been studied. Both human and bovine Fe-lactoferrins bound to the cells. Binding of bovine lactoferrin was inhibited by excess bovine lactoferrin but not by human lactoferrin, suggesting that the binding mechanisms for the two proteins are different. Binding of human but not bovine lactoferrin was inhibited by bovine lactoperoxidase, while a 20-fold excess of human IgA inhibited binding of human but not bovine lactoferrin. Human and bovine α-lactalbumins, bovine β-lactoglobulin, and human lysozyme had no effect on binding of lactoferrin from either species. Samples of bovine Fe- and apolactoferrin in capillary tubes were exposed to temperatures of 72 °C for 20 s, 85 °C for 20 min or 137 °C for 8 s. All the heated samples inhibited binding of native Fe- and apolactoferrin, though to a lesser extent than the native proteins. Both heated and native lactoferrins enhanced [3H]thymidine incorporation by U937 cells, except for Fe-lactoferrin heated at 85 °C for 20 min, which was inhibitory. These results suggest that heat treatment of lactoferrin under conditions used for industrial processing does not greatly affect its ability to interact with and stimulate monocytic cells, and that other milk proteins in general do not interfere with lactoferrin–monocyte interactions. It may thus be feasible to incorporate biologically active lactoferrin into infant formulas.
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Tomita, M., H. Wakabayashi, K. Yamauchi, S. Teraguchi, and H. Hayasawa. "Bovine lactoferrin and lactoferricin derived from milk: production and applications." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 109–12. http://dx.doi.org/10.1139/o01-230.

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Bovine lactoferrin is produced on an industrial scale from cheese whey or skim milk. The safety of purified lactoferrin has been confirmed from the results of a reverse mutation test using bacteria, a 13-week oral repeated-dose toxicity study in rats, and clinical studies. In order to apply active lactoferrin to various products, a process for its pasteurization was developed. Subsequently, lactoferrin has been used in a wide variety of products since it was first added to infant formula in 1986. A pepsin hydrolysate of lactoferrin is also used in infant formula. This hydrolysate contains a potent antimicrobial peptide named lactoferricin that is derived from the lactoferrin molecule by pepsin digestion. Semilarge-scale purification of lactoferricin can be performed by hydrophobic interaction chromatography. Lactoferricin also exhibits several biological actions and appears to be the functional domain of lactoferrin. Recent studies have demonstrated that oral administration of lactoferrin or lactoferricin exerts a host-protective effect in various animals and in humans. The results of these studies strongly suggest that the effects of oral lactoferrin are mediated by modulation of the immune system. Further elucidation of the clinical efficacy and mechanism of action of lactoferrin will increase the value of lactoferrin-containing products.Key words: bovine, lactoferrin, lactoferricin.
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Wang, Ye, James D. Morton, Alaa EL-Din A. Bekhit, Alan Carne, and Susan L. Mason. "Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin." Foods 10, no. 6 (June 7, 2021): 1305. http://dx.doi.org/10.3390/foods10061305.

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Although the bioactivities of bovine lactoferrin have been extensively investigated, little is known about deer milk lactoferrin bioactivity and its amino acid sequence. This research investigated the amino acid sequence of deer lactoferrin and the antimicrobial activities of two lactoferrin-encrypted peptides; lactoferricin (Lfcin) and lactoferrampin (Lfampin). Deer lactoferrin was found to have a molecular weight of 77.1 kDa and an isoelectric point of 7.99, which are similar to that of bovine lactoferrin, 78 kDa and pI 7.9. Deer lactoferrin contains 707 amino acids, one amino acid less than bovine lactoferrin, and has 92% homology with bovine lactoferrin. Deer lactoferricin exhibited strong antimicrobial activity against E. coli American Type Culture Collection (ATCC) 25922 and L. acidophilus ATCC 4356. The antimicrobial activities of deer and bovine Lfcin and Lfampin were compared. Based on MIC, deer Lfcin was found to be a more effective inhibitor of L. acidophilus ATCC 4356 than bovine Lfcin, but bovine Lfcin and Lfampin were more effective against E. coli ATCC 25922 than deer Lfcin and Lfampin. The deer Lfcin sequence differed at seven amino acids from bovine Lfcin and this decreased the net positive charge and increased the hydrophobicity. Deer Lfampin contained two differences in amino acid sequence compared to bovine Lfampin which decreased the net positive charge. These amino acid sequence differences likely account for differences in antibacterial activity. Positive charge and hydrophobic residues provide the amphipathic character of these helical peptides, and are considered important for binding of antimicrobial peptides. In silico modelling of deer Lfcin indicated an identical α-helical structure compared to bovine Lfcin.
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Steijns, Jan M., and A. C. M. van Hooijdonk. "Occurrence, structure, biochemical properties and technological characteristics of lactoferrin." British Journal of Nutrition 84, S1 (November 2000): 11–17. http://dx.doi.org/10.1017/s0007114500002191.

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The structure of the iron-binding glycoprotein lactoferrin, present in milk and other exocrine secretions, has been elucidated in great detail, both the three-dimensional protein structure and the attached N-glycans. Structure–function relationships are being established. From these studies a function for lactoferrin in host defence and modulation of iron metabolism emerges. This paper describes in some detail how iron and other cations may be bound by lactoferrins from human or bovine sources and elucidates parts of the molecule that are critical for interactions with cells and biomolecules. Furthermore, the technological aspects, more specifically the heat-sensitivity, of bovine lactoferrin in different matrices are described.
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Zaczyńska, Ewa, Jolanta Artym, Maja Kocięba, Timo Burster, Marian Kruzel, Maria Paprocka, and Michał Zimecki. "Antiviral Resistance of Splenocytes in Aged Mice." Polish Journal of Microbiology 66, no. 1 (March 30, 2017): 131–34. http://dx.doi.org/10.5604/17331331.1235002.

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We compared the susceptibility to viral infection of splenocytes, isolated from young versus old CBA mice, and evaluated the antiviral actions of lactoferrin in splenocytes infected with Encephalomyocarditis virus (EMCV). Recombinant mouse lactoferrin (rmLF) and bovine lactoferrin (bLF) were used. There were no differences in the susceptibility to EMCV infection in the studied age categories. Both types of lactoferrins were protective in young and old mice. The study confirmed the undisturbed viral resistance in old mice and the protective actions of lactoferrin in viral infection. The antiviral action of the homologous mouse lactoferrin was demonstrated for the first time.
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Yoo, Yung-Choon, Shikiko Watanabe, Ryosuke Watanabe, Katsusuke Hata, Kei-ichi Shimazaki, and Ichiro Azuma. "Bovine Lactoferrin and Lactoferricin, a Peptide Derived from Bovine Lactoferrin, Inhibit Tumor Metastasis in Mice." Japanese Journal of Cancer Research 88, no. 2 (February 1997): 184–90. http://dx.doi.org/10.1111/j.1349-7006.1997.tb00364.x.

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Kühnle, Andrea, Thomas Lütteke, Kim Bornhöfft, and Sebastian Galuska. "Polysialic Acid Modulates the Binding of External Lactoferrin in Neutrophil Extracellular Traps." Biology 8, no. 2 (March 28, 2019): 20. http://dx.doi.org/10.3390/biology8020020.

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Neutrophil extracellular traps (NETs) are formed by neutrophils during inflammation. Among other things, these DNA constructs consist of antimicrobial proteins such as lactoferrin and histones. With these properties, NETs capture and destroy invading microorganisms. The carbohydrate polysialic acid (polySia) interacts with both lactoferrin and histones. Previous experiments demonstrated that, in humans, lactoferrin inhibits the release of NET and that this effect is supported by polySia. In this study, we examined the interplay of lactoferrin and polySia in already-formed NETs from bovine neutrophils. The binding of polySia was considered to occur at the lactoferricin (LFcin)-containing domain of lactoferrin. The interaction with the peptide LFcin was studied in more detail using groups of defined polySia chain lengths, which suggested a chain-length-dependent interaction mechanism with LFcin. The LFcin domain of lactoferrin was found to interact with DNA. Therefore, the possibility that polySia influences the integration of lactoferrin into the DNA-structures of NETs was tested by isolating bovine neutrophils and inducing NETosis. Experiments with NET fibers saturated with lactoferrin demonstrated that polySia initiates the incorporation of external lactoferrin in already-loaded NETs. Thus, polySia may modulate the constituents of NET.
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Buchta, Richard. "Ovine lactoferrin: isolation from colostrum and characterization." Journal of Dairy Research 58, no. 2 (May 1991): 211–18. http://dx.doi.org/10.1017/s0022029900029757.

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SummaryHighly purified lactoferrin was isolated from ovine colostrum by sequential purification on CM-Sephadex C-50 and Blue-Sepharose, with overall yield of 55%. The ovine lactoferrin was characterized by SDS-PAGE, its amino acid composition and N-terminal sequence to residue 30. Homology with bovine and human lactoferrins was greater than 80 and 50% respectively. Antibodies to ovine lactoferrin were raised in rabbits and used to develop an enzyme-linked immuno-sorbent assay (ELISA). The antiserum was not cross reactive with other colostrum proteins.
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Mirayanti, Ni Luh Wayan Yulia, I. Gusti Ngurah Kade Mahardika, and Made Pharmawati. "Produksi Rekombinan Bovine Lactoferrin pada Sistem Ekspresi Eschericihia coli." Jurnal Veteriner 23, no. 1 (March 31, 2022): 105–11. http://dx.doi.org/10.19087/jveteriner.2022.23.1.105.

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Lactoferrin merupakan glikoprotein berukuran 80 kDa yang memiliki keunggulan dalam aktivitas biologis sebagai antimikroba, antibakteri, antivirus, antiparasit, hingga imunomodulator. Kemajuan bidang teknologi rekombinan memungkinkan untuk menghasilkan protein lactoferrin dalam skala besar, sehingga produksi rekombinan lactoferrin dapat dilakukan di berbagai sistem ekspresi. Escherichia coli menjadi salah satu inang pada sistem ekspresi yang banyak digunakan dalam produksi protein rekombinan. Rekombinan protein bovine lactoferrin diproduksi dengan penyisipan gen bovine lactoferrin pada plasmid pET 11-a. Gen bovine lactoferrin yang telah disisipkan dalam plasmid pET, selanjutnya ditransformasikan dan diekspresikan ke dalam sel inang E. coli BL21. Ekspresi protein bovine lactoferrin diinduksi dengan penambahan chaperone salah satu koekspresi, yang mendampingi sistem sintesis E.coli untuk mencapai ekspresi protein yang diinginkan. Ekspresi plasmid pET11a – Bovlacto dalam bakteri E.coli didukung oleh induser L-arabinosa dan IPTG. Gen bovine lactoferrin yang tersisip di dalam plasmid rekombinan pET-11a telah mampu diekspresikan dengan baik di dalam bakteri E.coli BL21 dengan adanya sinyal hibridisasi pada uji metode dot blot dan pita spesifik target yaitu pada kisaran posisi 80-85 kDa hasil elektroforesis SDS-PAGE.
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Kühnle, Andrea, Christina E. Galuska, Kristina Zlatina, and Sebastian P. Galuska. "The Bovine Antimicrobial Peptide Lactoferricin Interacts with Polysialic Acid without Loss of Its Antimicrobial Activity against Escherichia coli." Animals 10, no. 1 (December 18, 2019): 1. http://dx.doi.org/10.3390/ani10010001.

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The lactoferrin-derived peptide lactoferricin (LFcin) belongs to the family of antimicrobial peptides, and its bovine form has already been successfully applied to counteract enterohemorrhagic Escherichia coli (EHEC) infection. Recently, it was described that LFcin interacts with the sugar polymer polysialic acid (polySia) and that the binding of lactoferrin to polySia is mediated by LFcin, included in the N-terminal domain of lactoferrin. For this reason, the impact of polySia on the antimicrobial activity of bovine LFcin was investigated. Initially, the interaction of LFcin was characterized in more detail by native agarose gel electrophoresis, demonstrating that a chain length of 10 sialic acid residues was necessary to bind LFcin, whereas approximately twice-as-long chains were needed to detect binding of lactoferrin. Remarkably, the binding of polySia showed, independently of the chain length, no impact on the antimicrobial effects of LFcin. Thus, LFcin binds polySia without loss of its protective activity as an antimicrobial peptide.
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Dissertations / Theses on the topic "Bovine lactoferrin"

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Nam, Seung-Hee. "Affinity Purification of Bovine Lactoferrin and Bovine Transferrin from Using Immobilized Gangliosides." DigitalCommons@USU, 2000. https://digitalcommons.usu.edu/etd/5471.

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Bovine lactoferrin (BLF) and bovine transferrin (BTF) are major-iron transport and regulation proteins found in bovine whey. BLF and BTF must interact with the eukaryotic cell surface to mediate their biological function of iron delivery and cellular functions of inflammatory and immunological modulation. As common components of the eukaryotic cell surface, gangliosides were used for affinity purification of BLF and BTF. Bovine gangliosides were isolated from fresh buttermilk and covalently immobilized onto controlled-pore glass beads (66 μg/g beads). After the matrix was loaded with whey protein (WPI or WPC), lactoferrin was eluted with 1 M NaCl and lll identified by N-terminal protein sequencing. Pretreated whey isolate (1 % wt/vol) showed the highest lactoferrin purity with 40% among protein sources, and whey protein isolate (10% wt/vol) showed the highest recovery with 105%. Bovine transferrin was eluted with sodium phosphate buffers at pH 7 after the immobilized matrix was loaded with a 2% (wt/vol) whey solution. The ganglioside column resulted in a 74.2% recovery of BTF from whey, and the BTF was enriched to 61% purity after Mono-Q chromatography. Bovine transferrin was identified by SDS-PAGE analysis, Western analysis, and isoelectrofocusing. In conclusion, immobilized gangliosides can be used to purify BLF and BTF from bovine whey.
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Zhang, Norman Tianshu. "Isolation of lactoferrin from bovine colostrum by chromatographic techniques." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0010/MQ59911.pdf.

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Prgomet, Christian. "Lactoferrin: protective role in the bovine mammary gland and newborn calves." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=98032033X.

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Hogshead, Bradley Thomas. "Bovine Parainfluenza-3 Specific Antibodies in Veal Calves Supplemented with Cinnamaldehyde or Lactoferrin." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1512121726642402.

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Yamauchi, Koji. "Studies on host defense effects of bovine lactoferrin and its utilization as functional food materials." Kyoto University, 2000. http://hdl.handle.net/2433/151611.

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Goodman, Richard E. "Bovine mammary lactoferrin : cDNA cloning, Northern blots, and analysis of the mRNA sequence and deduced protein structure /." The Ohio State University, 1990. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487678444258466.

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Merrifield, Daniel Lee. "Evaluation of selected probiotics and bovine lactoferrin as feed supplements for rainbow trout (Oncorhynchus mykiss Walbaum) for applications in aquaculture." Thesis, University of Plymouth, 2009. http://hdl.handle.net/10026.1/614.

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A series of investigations were carried out to assessth e intestinal microbiota of rainbow trout and the potential applications of probiotics and bovine lactoferrin (M). Farm and aquarium reared rainbow trout were examined with specific emphasis on the autochthonous microbial communities. Culture-based, culture-independent and electron microscopical investigations revealed mixed, complex microbial communities in all intestinal regions. DGGE based analysis revealed unique species present either only as allochthonous populations or autochthonous populations. 16S rRNA sequence analysis allowed species level identification of a range of isolates, many of which have not been identified from the rainbow trout digestive tract previously. Two ftirther investigations were carried out to assess the potential of using commercial probiotics and bovine Lf on growth, feed utilisation, health and intestinal colonisation of rainbow trout. Standard commercial diets were supplemented with B. subtills, B. licheniformis and Enterococcus faecium either singularly or synergistically. When comparing the findings of the joint study it can be concluded that the application of probiotics with rainbow trout, and likely other finfish species, is highly complicated. Full intestinal replacement of indigenous microbiota is not likely to be a good idea when using E. faecium; the results indicate that a synergistic relationship with the indigenous microbiota is likely to be involved in providing host benefits. Bacillus probiotics only appeared to be effective at high intestinal levels indicating that a synergistic relationship with the indigenous microbiota may not be as important. T'he joint study also indicates that it is not always possible to reproduce probiotic benefits even when using the same probionts, the same fish species and similar rearing conditions. Thus, the physiological status of the fish and the indigenous microbiota are likely to play an important role in the outcome of probiotic administration. A subsequent trial was conducted to evaluate Pediococcus acidilactic! as a probiotic for rainbow trout. The experiment was conducted to supplement the diet with either vegetative cells or lyophilised powder (as commercially provided). Despite successful intestinal colonisation, irrelevant of supplementation form few significant benefits were observed. SEM of the posterior mucosa revealed a localised colonisation pattern of P. acidilactic! between the mucosal folds similar to the observed indigenous microbiota from the farmed fish. This revelation led to a further trial to investigate the nature of probiotic colonisation through the gastro-intestinal tract using electron microscopy. The study confirmed the high colonisation of P. acidilactici on the epithelium of the anterior intestine and posterior intestine. However, it was not possible to observe such colonisation with Bacillus spp. or E. faeclum; despite culture-based results to the contrary. It is likely that the true mucosal colonisation may sometimes be confused with colonisation of the mucus layer as opposed to actual attachment to the epithelium itself. Therefore, it is crucial to utilise electron microscopy in order to confirm epithelial colonisation. The nature of both the indigenous microbiota and the application of probiotics appears to be more complicated than previously thought and continued research is clearly warranted.
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Chand, Amita. "On-farm fractionation of milk components." The University of Waikato, 2006. http://hdl.handle.net/10289/2669.

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Methods for on-farm extraction of low-concentration (minor) proteins from raw whole bovine milk directly after milking were explored. These minor proteins have high commercial value. Lactoferrin (LF) and lactoperoxidase (LP) were used as model proteins for extraction using cation exchange chromatography. Laboratory fractionations showed that milk could be processed by conventional column chromatography without excessive column backpressures if resin with large particles sizes were used and the temperature was high enough so fat in the milk was malleable; ideally the milk should be near the secretion temperature of 37oC. Processing parameters such as equilibrium and dynamic capacities were determined for SP Sepharose ™ (GE Healthcare Technologies) and Bio Rex 70 (BioRad Laboratories) resins. SP Sepharose Big Beads (SP BB) were found to be more suitable than BR 70, for raw whole milk processing due to the larger size (200 um). Design considerations showed that column chromatography was not the most practical method for on-farm processing of fresh, raw whole milk. Trials with a single-stage stirred tank showed that SP BB resin could extract up to 65% of LF (initial LF concentration of 0.5 mg/mL) with a 10-minute adsorption time. The composite non-linear (CNL) model of Rowe et al. (1999) was used to describe LF uptake by SP BB resin in raw whole milk with initial LF concentrations of 0 to 1.0 mg/mL and resin:milk volume ratios of 0.010, 0.012, 0.017 and 0.024 over 45-minute contact times. The CNL model could be used to predict LF yields if initial feed concentration, milk and resin volumes, and contact times were known. Laboratory extractions showed that processing did not significantly affect bulk milk composition (fat, protein, lactose and total solids), indicating that the milk could be used for conventional processing after the minor proteins had been extracted. Resin cleaning and regeneration studies, using a procedure similar to that recommended by the resin supplier, showed that the Sepharose resin had not degraded and there was no significant decrease in binding capacity after 50 extraction cycles. A Protein Fractionation Robot (PFR) prototype based on a single-stage stirred tank and the operating parameters obtained from the laboratory trials was designed, assembled and coupled to an Automated Milking System (AMS) to process fresh, raw whole milk from individual cows immediately after milking. The LF and LP extracted from the milk from 16 individual cows were 19.7 - 55.2% (35.6 10.2%) and 21.2 - 99.5% (87.1 12.0%) respectively. Generally, higher extraction levels were obtained at higher resin:milk ratios. The amount of LF extracted on-farm agreed within 14.1 9.8% of those predicted by the CNL model, with predicted values generally being higher. The experimental on-farm adsorption values were calculated using data of LF recovered after elution, so differences between actual and predicted values may be due to losses during post-adsorption processing. Economic feasibility studies, based on experimental data from the PFR and realistic wholesale prices for LF and LP ($400 and $150/kg respectively) showed that PFR-based processing is economically viable if the farmer is paid for the LF and LP produced as well as the bulk milk. This system would have a payback period of approximately five years and an internal rate of return of 14.5%. Further case studies determined the sensitivity of the economics to various operating parameters and value/cost assumptions, including producing recombinant human protein from transgenic bovine milk. These studies showed that the higher the value of the processed raw milk, the higher the absorptive capacity of the resin, and the higher the value of the extracted protein, the more favourable the economics. In the extreme case of producing a very high value therapeutic protein (e.g. $20 000), the payback period could be as low as 0.3 years, with an internal rate of return of 818%.
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Ndiaye, Nafissatou. "Étude de la séparation de la lactoferrine bovine par électrodialyse avec membrane d'ultrafiltration." Thesis, Université Laval, 2009. http://www.theses.ulaval.ca/2009/26581/26581.pdf.

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Bédard, Sarah. "Étude de l'interaction entre la lactoferricine bovine et des monocouches de phospholipides." Thesis, Université Laval, 2007. http://www.theses.ulaval.ca/2007/24450/24450.pdf.

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Book chapters on the topic "Bovine lactoferrin"

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Bain, Heather, and John Tweedie. "Bovine Lactoferrin." In Lactoferrin Structure and Function, 231–33. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2548-6_23.

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Schanbacher, Floyd L., Surapon Pattanajitvilai, and Margaret C. Neville. "Posttranscriptional Regulation of Bovine and Human Lactoferrin." In Lactoferrin, 81–95. Totowa, NJ: Humana Press, 1997. http://dx.doi.org/10.1007/978-1-4612-3956-7_5.

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Teraguchi, Susumu, Kouichirou Shin, Kazuhiro Ozawa, Satoko Nakamura, Yasuo Fukuwatari, Seiichi Shimamura, and Mamoru Tomita. "Bacteriostatic Effects of Orally Administered Bovine Lactoferrin on Intestinal Bacteria in the Gut of Mice Fed Bovine Milk." In Lactoferrin, 303–12. Totowa, NJ: Humana Press, 1997. http://dx.doi.org/10.1007/978-1-4612-3956-7_19.

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Seyfert, Hans-Martin, Uta Klußmann, Uta Maria Steinhoff, Jens Vanselow, Dirk Koczan, and Gerd Hobom. "Variants and Biotechnological Use of the Bovine Lactoferrin-Encoding Gene." In Lactoferrin, 61–79. Totowa, NJ: Humana Press, 1997. http://dx.doi.org/10.1007/978-1-4612-3956-7_4.

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Wong, Henry, and Anthony B. Schryvers. "Construction of Recombinant Chimeric Human Lactoferrin/Bovine Transferrins." In Advances in Lactoferrin Research, 101–6. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4757-9068-9_12.

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Tomita, Mamoru, Koji Yamauchi, Susumu Teraguchi, and Hirotoshi Hayasawa. "Host Defensive Effects of Orally Administered Bovine Lactoferrin." In Advances in Lactoferrin Research, 189–97. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4757-9068-9_22.

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Shimazaki, Kei-ichi, Makoto Kamio, Myong Soo Nam, Shinji Harakawa, Tetsuya Tanaka, Yoshitaka Omata, Atsushi Saito, et al. "Structural and Immunochemical Studies on Bovine Lactoferrin Fragments." In Advances in Lactoferrin Research, 41–48. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4757-9068-9_5.

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Schoppe, I., C. A. Barth, and H. Hagemeister. "The Nutritive Value of Bovine Lactoferrin." In Milk Proteins, 108–9. Heidelberg: Steinkopff, 1989. http://dx.doi.org/10.1007/978-3-642-85373-9_16.

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Ogata, Tomohiro, Susumu Teraguchi, Kouichirou Shin, Michiko Kingaku, Yasuo Fukuwatari, Kouzou Kawase, Hirotoshi Hayasawa, and Mamoru Tomita. "The Mechanism of in Vivo Bacteriostasis of Bovine Lactoferrin." In Advances in Lactoferrin Research, 239–46. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4757-9068-9_28.

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Yoo, Yung-Choon, Shikiko Watanabe, Ryosuke Watanabe, Katsusuke Hata, Kei-ichi Shimazaki, and Ichiro Azuma. "Bovine Lactoferrin and LactoferricinTM Inhibit Tumor Metastasis in Mice." In Advances in Lactoferrin Research, 285–91. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4757-9068-9_35.

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Conference papers on the topic "Bovine lactoferrin"

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Barros, Caroline, Natália Ferreira, Jerson Silva, and Tuane Vieira. "bLf-PrP interaction: the antiprion effect of bovine lactoferrin." In International Symposium on Immunobiologicals. Instituto de Tecnologia em Imunobiológicos, 2022. http://dx.doi.org/10.35259/isi.2022_52259.

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Quan, Glen Lelyn, Kentaro Matsumiya, Michiaki Araki, Yasuki Matsumura, and Yoshihiko Hirata. "The role of sophorolipid as carrier of active substances." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/hnkx3869.

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Abstract:
Sophorolipid is a glycolipid-type biosurfactant, produced from natural sources by fermentation with a nonpathogenic yeast Starmerella bombicola. Its structure is composed of 2 hydrophilic parts, a sophorose unit, a glucose disaccharide glycosically linked to a hydroxyl fatty acid. Its structure spontaneously forms a vesicle of about 100 nm in an aqueous solution, which is similar to that of liposomes used as drug delivery systems and transdermal absorption promoters. It can be expected to have an effect of promoting permeation of active substances such as lactoferrin. Lactoferrin is an iron-binding glycoprotein having a molecular weight of about 80 kDa, and is most abundant in breast milk in the living body. Since it is also present in amniotic fluid that protects the mother and fetus, it is important to study the physiological relationship between skin and lactoferrin. The transdermal administration of lactoferrin with sophorolipid was verified, followed by the investigation protein-surfactant interactions between bovine lactoferrin and sophorolipid. Structural changes were further observed using spectroscopic, microscopic and biochemical methods under weakly acidic and neutral pH conditions. From particle size analysis by dynamic light scattering, microscopic observation by cryo-SEM, and digestion pattern observation by enzyme treatment, it was confirmed that bovine lactoferrin and sophorolipid interact with each other to form a sheet and nanometer-sized coagulation at pH 5.0 and 7.0 forming an aggregate, which was considered to be due to the self-organizing structure characteristic of sophorolipid. It can be concluded that sophorolipid has a potential of being a transport carrier of active substances, which can have vast applications not only in cosmetics but in drug delivery systems as well. Biosurfactants and biopolymers: Between interactions, orthogonality and mutual
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Liu, Hui-ping, Qing-quan Yan, Li Ma, Yi-wen Xu, and Ya Pei. "Notice of Retraction: Immunomodulatory Effects of Bovine Lactoferrin on BALB/C Mice." In 2011 5th International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2011. http://dx.doi.org/10.1109/icbbe.2011.5780067.

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Titov, E. I. "BIOTECHNOLOGY OF BOVINE LACTOFERIN FOR MEDICAL AND DIETARY PURPOSE." In 17th International Multidisciplinary Scientific GeoConference SGEM2017. Stef92 Technology, 2017. http://dx.doi.org/10.5593/sgem2017/61/s25.073.

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Wang, HaiKuan, XinHuai Zhao, RuiJuan Liu, Qi Wei, and FuPing Lu. "Heterologous Expression of Bovine Lactoferricin in Escherichia Coli." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.100.

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Deng, Qiang, Bate, Zhuoping Ding, Chengchu Liu, and Jianzhang Lu. "Preparation of an antibacterial peptide bovine lactoferricin by genetic engineering." In 2010 3rd International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2010. http://dx.doi.org/10.1109/bmei.2010.5639241.

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