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...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1967-06, Vol.242 (11), p.2577-2581
Main Authors: Cha, Sungman, Cha, Chung-Ja Mo, Parks, R.E.
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)99611-0