Zeitschriftenartikel zum Thema „Isoenzymes Analysis“
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Tillyer, C. R., S. Rakhorst und C. M. Colley. „Multicomponent analysis for alkaline phosphatase isoenzyme determination by multiple linear regression“. Clinical Chemistry 40, Nr. 5 (01.05.1994): 803–10. http://dx.doi.org/10.1093/clinchem/40.5.803.
Dunaway, G. A., T. P. Kasten, T. Sebo und R. Trapp. „Analysis of the phosphofructokinase subunits and isoenzymes in human tissues“. Biochemical Journal 251, Nr. 3 (01.05.1988): 677–83. http://dx.doi.org/10.1042/bj2510677.
Yoshikuni, Keiko, Takashi Matsuda, Janka Poracova, Akemi Sakai, Keiko Shimada, Noriko Tabuchi und Kiyoh Tanishima. „Phylogenic Study of Denaturation of Lactate Dehydrogenase Isoenzymes from Different Species by High and Low Temperature“. Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 38, Nr. 5 (September 2001): 548–53. http://dx.doi.org/10.1177/000456320103800513.
Giannoulaki, E. E., D. L. Kalpaxis, C. Tentas und P. Fessas. „Lactate dehydrogenase isoenzyme pattern in sera of patients with malignant diseases.“ Clinical Chemistry 35, Nr. 3 (01.03.1989): 396–99. http://dx.doi.org/10.1093/clinchem/35.3.396.
Bar, Jair, Stuart Spencer, Shethah Morgan, Laura Pike, David Cunningham, Jane D. Robertson, Juliane M. Jürgensmeier und Glenwood D. Goss. „Correlation of lactate dehydrogenase (LDH) isoenzyme profile with outcome in advanced colorectal cancer (CRC) patients (pts) treated with chemotherapy and bevacizumab (BEV) or cediranib (CED).“ Journal of Clinical Oncology 30, Nr. 15_suppl (20.05.2012): e13541-e13541. http://dx.doi.org/10.1200/jco.2012.30.15_suppl.e13541.
Pompeu, Georgia Bertoni, Priscila Lupino Gratão, Victor Alexandre Vitorello und Ricardo Antunes Azevedo. „Antioxidant isoenzyme responses to nickel-induced stress in tobacco cell suspension culture“. Scientia Agricola 65, Nr. 5 (2008): 548–52. http://dx.doi.org/10.1590/s0103-90162008000500015.
Kochhar, Sunita, Christopher B. Watkins, Patricia L. Conklin und Susan K. Brown. „A Quantitative and Qualitative Analysis of Antioxidant Enzymes in Relation to Susceptibility of Apples to Superficial Scald“. Journal of the American Society for Horticultural Science 128, Nr. 6 (November 2003): 910–16. http://dx.doi.org/10.21273/jashs.128.6.0910.
Singh, S. V., A. Kurosky und Y. C. Awasthi. „Human liver glutathione S-transferase ψ. Chemical characterization and secondary-structure comparison with other mammalian glutathione S-transferases“. Biochemical Journal 243, Nr. 1 (01.04.1987): 61–67. http://dx.doi.org/10.1042/bj2430061.
Maekawa, M., K. Sudo, K. Iwahara und T. Kanno. „Lactate dehydrogenase inhibition by immunoglobulin G in human serum.“ Clinical Chemistry 32, Nr. 7 (01.07.1986): 1347–49. http://dx.doi.org/10.1093/clinchem/32.7.1347.
Segil, N., A. Shrutkowski, M. B. Dworkin und E. Dworkin-Rastl. „Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence“. Biochemical Journal 251, Nr. 1 (01.04.1988): 31–39. http://dx.doi.org/10.1042/bj2510031.
DUJARDIN, J. C., A. L. BAÑULS, J. P. DUJARDIN, J. AREVALO, M. TIBAYRENC und D. LE RAY. „Comparison of chromosome and isoenzyme polymorphism in geographical populations of Leishmania (Viannia) peruviana“. Parasitology 117, Nr. 6 (Dezember 1998): 547–54. http://dx.doi.org/10.1017/s0031182098003357.
Palmieri, Gianna, Paola Giardina, Carmen Bianco, Bianca Fontanella und Giovanni Sannia. „Copper Induction of Laccase Isoenzymes in the Ligninolytic Fungus Pleurotus ostreatus“. Applied and Environmental Microbiology 66, Nr. 3 (01.03.2000): 920–24. http://dx.doi.org/10.1128/aem.66.3.920-924.2000.
Cousineau, J. C., A. K. Anderson, H. A. Daubeny und D. J. Donnelly. „Characterization of Red Raspberry Cultivars and Selections Using Isoenzyme Analysis“. HortScience 28, Nr. 12 (Dezember 1993): 1185–86. http://dx.doi.org/10.21273/hortsci.28.12.1185.
Pereira-Lorenzo, Santiago, Ana M. Ramos-Cabrer, Javier Ascasíbar-Errasti und Juan Piñeiro-Andión. „Analysis of Apple Germplasm in Northwestern Spain“. Journal of the American Society for Horticultural Science 128, Nr. 1 (Januar 2003): 67–84. http://dx.doi.org/10.21273/jashs.128.1.0067.
YOSHIMURA, Kazuya, Yukinori YABUTA, Masahiro TAMOI, Takahiro ISHIKAWA und Shigeru SHIGEOKA. „Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves“. Biochemical Journal 338, Nr. 1 (08.02.1999): 41–48. http://dx.doi.org/10.1042/bj3380041.
Iverson, A. J., A. Bianchi, A. C. Nordlund und L. A. Witters. „Immunological analysis of acetyl-CoA carboxylase mass, tissue distribution and subunit composition“. Biochemical Journal 269, Nr. 2 (15.07.1990): 365–71. http://dx.doi.org/10.1042/bj2690365.
Cousineau, J. C., und D. J. Donnelly. „Identification of Raspberry Cultivars in Vivo and in Vitro Using Isoenzyme Analysis“. HortScience 24, Nr. 3 (Juni 1989): 490–92. http://dx.doi.org/10.21273/hortsci.24.3.490.
Viallard, J. L., M. R. Ven Murthy und B. Dastugue. „Rapid electrophoretic determination of neuron-specific enolase isoenzymes in serum.“ Clinical Chemistry 32, Nr. 4 (01.04.1986): 593–97. http://dx.doi.org/10.1093/clinchem/32.4.593.
Cousineau, Johanne C., und Danielle J. Donnelly. „Use of Isoenzyme Analysis to Characterize Raspberry Cultivars and Detect Cultivar Mislabeling“. HortScience 27, Nr. 9 (September 1992): 1023–25. http://dx.doi.org/10.21273/hortsci.27.9.1023.
Ahmad, Riaz, Nazia Nazam, Arshad Khan und Mumtaz Alam. „Significance of Serum Lactate Dehydrogenase and its Isoenzymes During Post-Burn Follow-Up“. Journal of Medical Biochemistry 28, Nr. 3 (01.07.2009): 176–83. http://dx.doi.org/10.2478/v10011-009-0018-7.
Cousineau, Johanne C., und Danielle J. Donnelly. „Genetic Analysis of Isoenzymes in Raspberry“. Journal of the American Society for Horticultural Science 117, Nr. 6 (November 1992): 996–99. http://dx.doi.org/10.21273/jashs.117.6.996.
NOVELLI, G., F. CATIZONE und B. DALLAPICCOLA. „Analysis of isoenzymes in trophoblast cells“. Cell Biology International Reports 10, Nr. 3 (März 1986): 149. http://dx.doi.org/10.1016/s0309-1651(86)80003-0.
Scott, Joseph W., Farris L. Poole und Michael W. W. Adams. „Characterization of Ten Heterotetrameric NDP-Dependent Acyl-CoA Synthetases of the Hyperthermophilic ArchaeonPyrococcus furiosus“. Archaea 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/176863.
Redling, Stephanie, Imke L. Pfaff, Michael Leitges und Volker Vallon. „Immunolocalization of protein kinase C isoenzymes α, βI, βII, δ, and ε in mouse kidney“. American Journal of Physiology-Renal Physiology 287, Nr. 2 (August 2004): F289—F298. http://dx.doi.org/10.1152/ajprenal.00273.2003.
Lessard, F., und R. Dion. „Analysis for alpha-amylase isoenzymes by automated isoelectric focusing.“ Clinical Chemistry 35, Nr. 10 (01.10.1989): 2116–18. http://dx.doi.org/10.1093/clinchem/35.10.2116.
Ivashchenko, D. V., A. S. Osipov, E. V. Nazarova, M. A. Ovchinnikova, N. I. Buromskaya, V. V. Smirnov, P. V. Shimanov et al. „Efficacy and safety of antipsychotics in adolescents with an acute psychotic episode in relation to the activity of CYP3A and CYP2D6 isoenzymes“. Neurology, Neuropsychiatry, Psychosomatics 12, Nr. 6 (12.12.2020): 11–18. http://dx.doi.org/10.14412/2074-2711-2020-6-11-18.
Wyss, M., D. Maughan und T. Wallimann. „Re-evaluation of the structure and physiological function of guanidino kinases in fruitfly (Drosophila), sea urchin (Psammechinus miliaris) and man“. Biochemical Journal 309, Nr. 1 (01.07.1995): 255–61. http://dx.doi.org/10.1042/bj3090255.
Hoesch, R. M., und T. D. Boyer. „Purification and characterization of hepatic glutathione S-transferases of rhesus monkeys. A family of enzymes similar to the human hepatic glutathione S-transferases“. Biochemical Journal 251, Nr. 1 (01.04.1988): 81–88. http://dx.doi.org/10.1042/bj2510081.
Medh, R. D., M. Saxena, S. S. Singhal, H. Ahmad und Y. C. Awasthi. „Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8“. Biochemical Journal 278, Nr. 3 (15.09.1991): 793–99. http://dx.doi.org/10.1042/bj2780793.
Schultz, Carolyn J., Meier Hsu, Barbara Miesak und Gloria M. Coruzzi. „Arabidopsis Mutants Define an in Vivo Role for Isoenzymes of Aspartate Aminotransferase in Plant Nitrogen Assimilation“. Genetics 149, Nr. 2 (01.06.1998): 491–99. http://dx.doi.org/10.1093/genetics/149.2.491.
Lebherz, H. G., T. Burke, J. E. Shackelford, J. E. Strickler und K. J. Wilson. „Specific proteolytic modification of creatine kinase isoenzymes. Implication of C-terminal involvement in enzymic activity but not in subunit-subunit recognition“. Biochemical Journal 233, Nr. 1 (01.01.1986): 51–56. http://dx.doi.org/10.1042/bj2330051.
Arenas, J., V. Diaz, G. Liras, E. Gutierrez, I. Santos, A. Martinez und J. M. Culebras. „Activities of creatine kinase and its isoenzymes in serum in various skeletal muscle disorders.“ Clinical Chemistry 34, Nr. 12 (01.12.1988): 2460–62. http://dx.doi.org/10.1093/clinchem/34.12.2460.
Maekawa, Masato, Motoko Inomata, Masao S. Sasaki, Akihiro Kaneko, Mineko Ushiama, Kokichi Sugano, Jun Takayama und Takashi Kanno. „Electrophoretic Variant of a Lactate Dehydrogenase Isoenzyme and Selective Promoter Methylation of the LDHA Gene in a Human Retinoblastoma Cell Line“. Clinical Chemistry 48, Nr. 11 (01.11.2002): 1938–45. http://dx.doi.org/10.1093/clinchem/48.11.1938.
ICHIMURA, Michio, Rika EIKI, Keiko OSAWA, Satoshi NAKANISHI und Hiroshi KASE. „KS-505a, an isoform-selective inhibitor of calmodulin-dependent cyclic nucleotide phosphodiesterase“. Biochemical Journal 316, Nr. 1 (15.05.1996): 311–16. http://dx.doi.org/10.1042/bj3160311.
Bogaards, J. J. P., B. van Ommen und P. J. V. van Bladeren. „Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea“. Biochemical Journal 286, Nr. 2 (01.09.1992): 383–88. http://dx.doi.org/10.1042/bj2860383.
DEWASTE, Valérie, Valérie POUILLON, Colette MOREAU, Stephen SHEARS, Kazunaga TAKAZAWA und Christophe ERNEUX. „Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C“. Biochemical Journal 352, Nr. 2 (24.11.2000): 343–51. http://dx.doi.org/10.1042/bj3520343.
Rahayu, Sri, Sutiman Bambang Sumitro, T. Susilawati und Soemarno Soemarno. „ANALISIS ISOENZIM UNTUK MEMPELAJARI VARIASI GENETIK SAPI BALI DI PROVINSI BALI“. Berkala Penelitian Hayati 12, Nr. 1 (31.12.2006): 1–5. http://dx.doi.org/10.23869/bphjbr.12.1.20061.
Tillyer, C. R. „Error estimation in the quantification of alkaline phosphatase isoenzymes by selective inhibition methods.“ Clinical Chemistry 34, Nr. 12 (01.12.1988): 2490–93. http://dx.doi.org/10.1093/clinchem/34.12.2490.
Morikawa, Toshinobu. „Monosomic analysis of leaf peroxidase Px0 and Px9 loci in hexaploid oats“. Genome 30, Nr. 2 (01.04.1988): 99–102. http://dx.doi.org/10.1139/g88-017.
Naito, Eiji, Roka Shimada und Masashi Yuki. „Diagnostic utility of measuring lactate dehydrogenase levels and its isoenzyme activities for the evaluation of malignancy in feline pleural effusion and ascitic fluid“. Open Veterinary Journal 12, Nr. 5 (2022): 735. http://dx.doi.org/10.5455/ovj.2022.v12.i5.19.
Di Ilio, C., A. Aceto, T. Bucciarelli, S. Angelucci, M. Felaco, A. Grilli und G. Federici. „Glutathione transferase isoenzymes from human prostate“. Biochemical Journal 271, Nr. 2 (15.10.1990): 481–85. http://dx.doi.org/10.1042/bj2710481.
Higashiyama, M., S. Doi, N. Tomita, T. Monden, M. Murotani, Y. Kawasaki, T. Kobayashi, T. Shimano, M. Ogawa und S. Takai. „Immunohistochemical analysis of amylase isoenzymes in thyroid cancer.“ Journal of Clinical Pathology 44, Nr. 2 (01.02.1991): 144–46. http://dx.doi.org/10.1136/jcp.44.2.144.
Marretto, Jesila Pinto M., und Sonia G. Andrade. „Biochemical behavior of Trypanosoma cruzi strains isolated from mice submitted to specific chemotherapy“. Revista da Sociedade Brasileira de Medicina Tropical 27, Nr. 4 (Dezember 1994): 209–15. http://dx.doi.org/10.1590/s0037-86821994000400002.
Kazmierczak, S. C., W. J. Castellani, F. Van Lente, E. D. Hodges und B. Udis. „Effect of reticulocytosis on lactate dehydrogenase isoenzyme distribution in serum: in vivo and in vitro studies“. Clinical Chemistry 36, Nr. 9 (01.09.1990): 1638–41. http://dx.doi.org/10.1093/clinchem/36.9.1638.
Reddy, M. K., G. D. Heda und J. K. Reddy. „Purification and characterization of α-amylase from rat pancreatic acinar carcinoma. Comparison with pancreatic α-amylase“. Biochemical Journal 242, Nr. 3 (15.03.1987): 681–87. http://dx.doi.org/10.1042/bj2420681.
Hultberg, B., A. Isaksson, A. Lindgren, B. Israelsson und L. Brattström. „β-Hexosaminidase Isoenzymes A and B in Middle-Aged and Elderly Subjects: Determinants of Plasma Levels and Relation to Vascular Disease“. Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 33, Nr. 5 (September 1996): 432–37. http://dx.doi.org/10.1177/000456329603300506.
MITCHELL, Alyson E., Dexter MORIN, Jeffrey LAKRITZ und A. Daniel JONES. „Quantitative profiling of tissue- and gender-related expression of glutathione S-transferase isoenzymes in the mouse“. Biochemical Journal 325, Nr. 1 (01.07.1997): 207–16. http://dx.doi.org/10.1042/bj3250207.
Zoellner, H. F., und N. Hunter. „Histochemical identification of the vascular endothelial isoenzyme of alkaline phosphatase.“ Journal of Histochemistry & Cytochemistry 37, Nr. 12 (Dezember 1989): 1893–98. http://dx.doi.org/10.1177/37.12.2584695.
Zhou, Yixing, Michele R. Wing, John Sondek und T. Kendall Harden. „Molecular cloning and characterization of PLC-η2“. Biochemical Journal 391, Nr. 3 (25.10.2005): 667–76. http://dx.doi.org/10.1042/bj20050839.
Bialer, M. G., D. E. Bruns und T. E. Kelly. „Muscle enzymes and isoenzymes in Emery-Dreifuss muscular dystrophy“. Clinical Chemistry 36, Nr. 3 (01.03.1990): 427–30. http://dx.doi.org/10.1093/clinchem/36.3.427.