| Literature DB >> 5866654 |
Abstract
The total lactate dehydrogenase (LDH) in whole homogenates of various human tissues reacts more similarly toward pyruvate and lactate at 25 degrees C than expected from the marked differences in substrate inhibition at this temperature between isolated, purified LDH-1, and LDH-5. At 37 degrees 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.Entities:
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Year: 1965 PMID: 5866654 DOI: 10.1126/science.150.3703.1590
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728