PURIFICATION AND SOME PROPERTIES OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE FROM RABBIT SKELETAL MUSCLE MITOCHONDRIA

作     者：施善平 刘建华 林其谁 SHI SHANPING LIU JIANHUA LIN QISHUI (Shanghai Institute of Biochemistry, Academia Sinica)

作者机构：Shanghai Institute of Biochemistry Academia Sinica 

出 版 物：《Science in China,Ser.B》 (中国科学B辑(英文版))

年 卷 期：1986年第29卷第10期

页      面：1027-1038页

核心收录：

学科分类：1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学] 

主　　题：FAD PURIFICATION AND SOME PROPERTIES OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE FROM RABBIT SKELETAL MUSCLE MITOCHONDRIA DEAE der Pro 

摘      要：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 and a sedimentation coefficient of 10.7S. There were 1.7mg Triton X-100 and 26 μg 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.