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Science 16 September 1966:
Vol. 153. no. 3742, pp. 1411 - 1413
DOI: 10.1126/science.153.3742.1411
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Articles

Peafowl Lactate Dehydrogenase: Problem of Isoenzyme Identification

Richard G. Rose 1 and Allan C. Wilson 1

1 Department of Biochemistry, University of California, Berkeley

Peafowl, like other vertebrates, contain multiple forms of lactate dehydrogenase. The electrophoretic properties of the peafowl isoenzymes are unusual in that the isoenzyme from heart tissue can be either more or less anodic than that of muscle, depending on the pH. This finding focuses attention on the problem of isoenzyme identification. It is suggested that isoenzymes be identified on the basis of properties that are chemically and biologically more significant than electrophoretic mobility.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Phenoxyethanol: Protein Preservative for Taxonomists.
M. Nakanishi, A. C. Wilson, R. A. Nolan, G. C. Gorman, and G. S. Bailey (1969)
Science 163, 681-683
   Abstract »    PDF »
Embryonic Enzyme Patterns: Characterization of the Single Lactate Dehydrogenase Isozyme in Preimplanted Mouse Ova.
J. Rapola and O. Koskimies (1967)
Science 157, 1311-1312
   Abstract »    PDF »
Molecular Size of Hagfish Muscle Lactate Dehydrogenase.
N. Arnheim Jr., G. T. Cocks, and A. C. Wilson (1967)
Science 157, 568-569
   Abstract »    PDF »
Enzymatic Identification of Fish Products.
A. C. Wilson, G. B. Kitto, and N. O. Kaplan (1967)
Science 157, 82-83
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)