Unknown

Dataset Information

0

Purification and properties of L(+)-lactate dehydrogenase from potato tubers.


ABSTRACT: 1. A purification of l(+)-lactate dehydrogenase is described. 2. The final preparation is active with NADH and NADPH and with a number of keto acids, but evidence is presented to support the view that a single enzyme is involved. 3. NAD(+) showed product inhibition, but at slightly acid pH values there was evidence of co-operative binding. 4. At acid pH values ATP was a potent inhibitor and appears to be an allosteric effector. At neutral or alkaline pH values ATP behaved as a weak competitive inhibitor. 5. The physiological significance of inhibition by ATP is discussed.

SUBMITTER: Davies DD 

PROVIDER: S-EPMC1174228 | biostudies-other | 1972 Oct

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1165824 | biostudies-other
| S-EPMC8972991 | biostudies-literature
| S-EPMC3594981 | biostudies-literature
2008-02-13 | GSE10483 | GEO
| S-EPMC1176584 | biostudies-other
| S-EPMC1177158 | biostudies-other
| S-EPMC10997820 | biostudies-literature
| S-EPMC3064541 | biostudies-literature
2021-06-22 | GSE178602 | GEO
| S-EPMC7830743 | biostudies-literature