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[Isolation and characterization of lactate dehydrogenase from white fin muscles of the skate Raja clavata].

Authors
Type
Published Article
Journal
Ukrainskiĭ biokhimicheskiĭ zhurnal (1978)
Publication Date
Volume
62
Issue
6
Pages
38–42
Identifiers
PMID: 2087791
Source
Medline
License
Unknown

Abstract

Lactate dehydrogenase (LDH) from white driving muscle of skate Raja clavata was purified by the differential precipitation of ammonium sulphate between 52 and 55% saturation. Only one protein band with the LDH activity was obtained by nondenaturing electrophoresis. The same result was obtained by the SDS-electrophoresis. The relative molecular weight calculated by this method in the presence of DS-Na was 34 kDa; Km was 29 +/- 7 and 71 +/- 16 microM for NAD.H and pyruvate, respectively. The reaction was maximally activated by 0.8-6.0 mM pyruvate and inhibited in the regions above this level. Dilution of LDH below concentration of 1 microgram/ml reduced the enzyme activity. The pH-optimum for the LDH activity ranged 7.0-8.0.

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