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Science 17 December 1965:
Vol. 150. no. 3703, pp. 1590 - 1593
DOI: 10.1126/science.150.3703.1590
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Articles

Lactate Dehydrogenase Isozymes: Substrate Inhibition in Various Human Tissues

Elliot S. Vesell 1

1 Nationail Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland

The total lactate dehydrogenase (LDH) in whole homogenates of various human tissues reacts more similarly toward pyruvate and lactate at 25°C than expected from the marked differences in substrate inhibition at this temperature between isolated, purified LDH-1, and LDH-5. At 37°C, LDH-5 closely resembles LDH-1 in extent of inhibition by substrate. These results are incompatible with the theory that differences in degree of isozyme inhibition by substrate have resulted in predominance of LDH-5 in aerobic tissues and predominance of LDH-1 in aerobic tissues.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Pyruvate Inhibition of Lactate Dehydrogenase Activity in Human Tissue Extracts.
A. L. Latner, S. A. Siddiqui, and A. W. Skillen (1966)
Science 154, 527-529
   Abstract »    PDF »
Peafowl Lactate Dehydrogenase: Problem of Isoenzyme Identification.
R. G. Rose and A. C. Wilson (1966)
Science 153, 1411-1413
   Abstract »    PDF »


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