Affinity purification and subunit structure of soya bean lactate dehydrogenase

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

Phytochemistry 20(9): 2117-2121


ISSN/ISBN: 0031-9422
DOI: 10.1016/0031-9422(81)80096-9
Accession: 000815299

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Lactate dehydrogenase from soyabean was purified to homogeneity by affinity chromatography. The enzyme was purified by sequential adsorption on to Blue Sepharose and ATP-Sepharose followed by specific elution from each adsorbent by NADH. The enzyme preparations obtained by this double affinity purification were 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 was a tetramer with only one subunit type. In contrast to lactate dehydrogenase from several other plant sources, no isoenzymes were detectable.