The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Sites and patterns of protein and amino acid utilization during the spawning migration of salmon
Abstract
Some aspects of the biochemistry of sockeye salmon (Oncorhynchns nerka) were investigated during spawning migration in the Fraser River, B.C. Studies included measurements of the activities of metabolic enzymes, protein content, and free amino acid concentrations in various tissues. In white muscle, soluble and insoluble protein decreased by 70% during migration and the activities of most of the enzymes studied showed a similar pattern. In contrast, the activities of cathepsin D (EC 3.4.23.5) and carboxypeptidase A (EC 3.4.12A.1) increased considerably, whereas the activities of alanine aminotransferase (EC 2.6.1.2) and malic enzyme (EC 1.1.1.40) were unchanged during migration. In red muscle and heart there was little change in either protein levels or enzyme activities, with the exception of glucose-6-phosphate dehydrogenase (EC 1.1.1.4), which increased threefold to sixfold. In liver, the activities of metabolic enzymes and the levels of soluble protein decreased, whereas proteolytic enzyme activities increased slightly during migration.It is concluded that white muscle is the primary source of the amino acids utilized during migration. A model is proposed to account for the fate of the amino acids released by proteolysis in white muscle. It is suggested that most of the amino acids are collected as alanine and transported to other tissues in this form.
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Cites
THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN
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The origin of alanine produced in skeletal muscle.
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Garber, A. J., Karl, I. E., & Kipnis, D. M. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33860-7 · Cited by 201
Petrescu, I., Bojan, O., Saied, M., Bârzu, O., Schmidt, F. H., & Kühnle, H. F. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90582-7 · Cited by 113
Cathepsin D: Rapid Isolation by Affinity Chromatography on Haemoglobin‐Agarose Resin
Smith, R., & Türk, V. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03762.x · Cited by 97
Metabolic Sources of Heat and Power in Tuna Muscles
Guppy, M., Hulbert, W. C., & Hochachka, P. W. (1979) · Journal of Experimental Biology · doi:10.1242/jeb.82.1.303 · Cited by 94
Self-citationKarl, I. E., Garber, A. J., & KIPNIS, D. M. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33861-9 · Cited by 82
Alanine biosynthesis during starvation in skeletal muscle of the spiny dogfish, Squalus acanthias
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Self-citationTHE TUNA POWER PLANT AND FURNACE
Hochachka, P. W., Hulbert, W. C., & Guppy, M. (1978) · Elsevier eBooks · doi:10.1016/b978-0-12-639180-0.50017-3 · Cited by 47
Self-citationCowey, C. B., Brown, D. A., Adron, J. W., & Shanks, A. M. (1974) · Marine Biology · doi:10.1007/bf00387299 · Cited by 32
Relative anaerobic glycolytic capacity and pyruvate kinase activity of rabbit tissues
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[15] 3-ketoacid CoA-transferase
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Cited by
Cortisol in teleosts: dynamics, mechanisms of action, and metabolic regulation
Mommsen, T. P., Vijayan, M. M., & Moon, T. W. (1999) · Reviews in Fish Biology and Fisheries · doi:10.1023/a:1008924418720 · Cited by 2,324
Self-citationLi, P., Mai, K., Trushenski, J., & Wu, G. (2009) · Amino Acids · doi:10.1007/s00726-008-0171-1 · Cited by 908
Some insights into energy metabolism for osmoregulation in fish
Tseng, Y.-C., & Hwang, P.-P. (2008) · Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology · doi:10.1016/j.cbpc.2008.04.009 · Cited by 470
Ammonia toxicity, tolerance, and excretion
Ip, Y. K., Chew, S. F., & Randall, D. J. (2001) · Fish Physiology · doi:10.1016/s1546-5098(01)20005-3 · Cited by 360
The constraints on cephalopods: why squid aren't fish
O'Dor, R. K., & Webber, D. M. (1986) · Canadian Journal of Zoology · doi:10.1139/z86-241 · Cited by 275
Metadata
- Authors
- Mommsen, T. P., French, C. J., & Hochachka, P. W.
- Venue
- Canadian Journal of Zoology
- Publisher
- Canadian Science Publishing
- Published
- 1980-10-01
- Volume
- 58
- Issue
- 10
- Pages
- 1785-1799
- ISSN
- 0008-4301 (ISSN-L)
- 1480-3283
- OpenAlex
- W2163345765
- Cited by
- 371
- References
- 14
- FWCI
- 11.62
- Type
- journal article
- Language
- en
- Open access
- closed
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