Section 44
Chapter 43,219

H4-isozyme of lactate dehydrogenase in the solution of sodium chloride--3. the enzymatic activity and the pyruvate inhibition

Yamamoto, S.

International Journal of Biochemistry 15(2): 185-190


ISSN/ISBN: 0020-711X
PMID: 6822318
DOI: 10.1016/0020-711x(83)90064-2
Accession: 043218693

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1. Low enzymatic activities in low pyruvate concentrations and high Km were observed in sodium chloride solutions. 2. The pyruvate inhibition shown by the % activity at 1 mM pyruvate was lower sodium chloride than in 0.1 M sodium phosphate. 3. At 40 degrees C, as compared with results at 20 degrees C, less pyruvate inhibition was observed in phosphate buffer and in sodium chloride solutions. 4. By using the equilibrium constants between dimer and tetramer, a theoretical explanation is proposed for the pyruvate inhibition. In this explanation, it is suggested that the quaternary complex which is composed of tetrameric enzyme, coenzyme and two kinds of pyruvates was the main cause of the pyruvate inhibition.

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