Purification and some properties of glycerol-3-phosphate dehydrogenase from rabbit skeletal muscle mitochondria.
Sci Sin B
; 29(10): 1027-38, 1986 Oct.
Article
in En
| MEDLINE
| ID: mdl-3576173
ABSTRACT
Glycerol-3-phosphate dehydrogenase (E. C. 1. 1. 99. 5) was solubilized from rabbit skeletal muscle mitochondria by Triton X-100 and purified through hydroxyapatite column chromatography, DEAE-Sepharose CL-6B column chromatography and sucrose density gradient ultracentrifugation. The preparation was electrophoretically pure, the total recovery was 10% and the specific activity had been increased 200-fold. The apparent molecular weight of the enzyme polypeptide was 69,000, it existed in the form of enzyme-Triton X-100 complex with a Stokes' radius of 59 A and a sedimentation coefficient of 10.7 S. There were 1.7 mg Triton X-100 and 26 micrograms phospholipid per mg protein of the preparation. The enzyme absorbed at 410 and 460 nm which could be attributed to non-haem iron and FAD respectively. Both of the absorption would be largely diminished by adding the substrate glycerol-3-phosphate.
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Database:
MEDLINE
Main subject:
Glycerolphosphate Dehydrogenase
/
Mitochondria, Muscle
Limits:
Animals
Language:
En
Journal:
Sci Sin B
Year:
1986
Type:
Article