Succinic Thiokinase
A method of purification of succinic thiokinase from pig hearts is described by which a 700- to 800-fold purification over the crude extract may be achieved with about 10% recovery. The final product has a specific activity of about 110 µ m units per mg, and the molecular weight of the enzyme is es...
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| Published in | The Journal of biological chemistry Vol. 242; no. 11; pp. 2577 - 2581 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
American Society for Biochemistry and Molecular Biology
10.06.1967
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| Online Access | Get full text |
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| Summary: | A method of purification of succinic thiokinase from pig hearts is described by which a 700- to 800-fold purification over
the crude extract may be achieved with about 10% recovery. The final product has a specific activity of about 110 µ m units per mg, and the molecular weight of the enzyme is estimated as about 70,000. The stability of the enzyme at various
pH values is presented. Two previously unobserved reactions catalyzed by the enzyme are described. The relative rates of catalysis
of the normal reaction, the coenzyme A-dependent arsenolysis of guanosine triphosphate, and the succinate-dependent guanosine
triphosphatase are approximately 1, 0.008, and 0.0004 respectively. Substrate activities of 6-thioguanosine triphosphate and
dephospho-coenzyme A are described. |
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| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1016/S0021-9258(18)99611-0 |