Jump to: Page Content, Section Navigation, Site Navigation, Site Search, Account Information, or Site Tools.
|
|
Articles
Lactate Dehydrogenase Isozymes: Substrate Inhibition in Various Human Tissues
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:
|
Science. ISSN 0036-8075 (print), 1095-9203 (online)