DIAPHORASE-LIKE ENZYME IN CULTURE FILTRATE OF CLOSTRIDIUM PERFRINGENS BP6K
1958 Volume 2 Issue 1 Pages 39-46
Details
1958 Volume 2 Issue 1 Pages 39-46
1. From the culture filtrate of Cl. perfringens type A strain BP6K, a diaphorase-like enzyme, was isolated.
2. The enzyme oxidized DPNH in the presence of 2.6-DPIP, methylene blue, and menadione but not in the presence of oxygen, nitrate, nitrite, ferricyanide, gluthathione, fumarate, pyruvate, formate, formaldehyde, α-ketoglutarate, xanthine, and cytochrome c.
3. The enzyme did not oxidize TPNH in the presence of 2.6-DPIP.
4. The optimal pH of this enzyme was 8.0.
5. The enzyme was most stable at pH 5.0.
6. Temperature coefficient (Q10) of the enzyme fell between 1.56 and 2.2.
7. Antimycin inhibited enzyme activity by 11% at 2.7×10-4M, and sodium azide 23% at 5.12×10-4M.
8. The Michaelis constant of this enzyme for DPNH was 2.53×10-4M.
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