Affinity purification and subunit structure of soybean glycine max lactate dehydrogenase

Jervis, L.; Robertson, E.R.; Schmidt, C.N.G.

Phytochemistry (Oxford) 20(9): 2117-2122

1981


ISSN/ISBN: 0031-9422
Accession: 004685845

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Abstract
The lactate dehydrogenase (LDH) from soybean was purified to homogeneity by affinity chromatography. The enzyme was purified by sequential adsorption onto blue Sepharose and ATP-Sepharose followed by specific elution from each adsorbent by NADH. The enzyme preparations obtained by this double affinity purification was purified over 17,000-fold and were homogeneous as judged by polyacrylamide gel electrophoresis under denaturing and non-denaturing conditions. The overall recovery of enzyme was high and the purification procedure was rapid. The enzyme is a tetramer with only 1 subunit type. In contrast to LDH from several other plant sources, no isoenzymes were detectable.