Rauchová H, Beleznai Z, Drahota Z
Institute of Physiology, Czechoslovakian Academy of Sciences, Prague.
J Bioenerg Biomembr. 1988 Oct;20(5):623-32. doi: 10.1007/BF00768923.
Mitochondrial L-glycerol-3-phosphate dehydrogenase (E.C. 1.1.99.5.) was studied by chemical modification in situ with different amino acid side chain specific reagents in mitochondria isolated from hamster brown adipose tissue. The SH-modifying reagents have only slight effect on the enzyme activity. The most effective chemicals were tetranitromethane and diazobenzene sulfonic acid. The enzyme activity can be abolished completely by both of them. In the presence of Ca2+ and/or glycerol-3-phosphate inhibition was greater at the same electrophilic reagent concentration. The effect of Ca2+ and glycerol-3-phosphate is nonadditive on inhibition by these reagents.
采用不同的氨基酸侧链特异性试剂,对从仓鼠棕色脂肪组织分离的线粒体中的线粒体L-3-磷酸甘油脱氢酶(E.C. 1.1.99.5.)进行原位化学修饰研究。SH修饰试剂对该酶活性仅有轻微影响。最有效的化学试剂是四硝基甲烷和重氮苯磺酸。它们均可使酶活性完全丧失。在相同亲电试剂浓度下,Ca2+和/或3-磷酸甘油存在时抑制作用更强。Ca2+和3-磷酸甘油对这些试剂抑制作用的影响并非相加性的。