Unknown

Dataset Information

0

Isolation of human lactate dehydrogenase isoenzyme X by affinity chromatography.


ABSTRACT: Human isoenzyme LDH-X (lactate dehydrogenase isoenzyme X) was isolated from seminal fluid of frozen semen samples by affinity chromatography by using oxamate-Sepharose and AMP-Sepharose. In the presence of 1.6 mM-NAD+, isoenzyme LDH-X does not bind to AMP-Sepharose, whereas the other lactate dehydrogenase isoenzymes do. This is the crucial point in the isolation of isoenzyme LDH-X from the other isoenzymes. The purified human isoenzyme LDH-X had a specific activity of 146 units/mg of protein.

SUBMITTER: Kolk AH 

PROVIDER: S-EPMC1185842 | biostudies-other | 1978 Sep

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1163336 | biostudies-other
| S-EPMC1177729 | biostudies-other
| S-EPMC5531073 | biostudies-literature
| S-EPMC4730284 | biostudies-literature
| S-EPMC1163192 | biostudies-other
| S-EPMC1172559 | biostudies-other
| S-EPMC1183998 | biostudies-other
| S-EPMC110528 | biostudies-literature
| S-EPMC6443703 | biostudies-literature
| S-EPMC1172411 | biostudies-other