[Isolation and characterization of lactate dehydrogenase from white fin muscles of the skate Raja clavata].
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.
Lushchak
V I
VI
D000818:Animals; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid; D012860:Skates, Fish / Q000378:metabolism*
D011773:Pyruvates; D009243:NAD; D019289:Pyruvic Acid; D007770:L-Lactate Dehydrogenase
Vydelenie i kharakteristika laktatdegidrogenazy iz belykh plavnikovykh myshts skata Raja clavata.