Bodenstein-Lang J, Buch A, Follmann H
Fachbereich Chemie, Arbeitsgruppe Biochemie der Phillipps-Universität,Marburg, FRG.
FEBS Lett. 1989 Nov 20;258(1):22-6. doi: 10.1016/0014-5793(89)81606-0.
Thioredoxins have been purified from pig heart and potato tuber mitochondria which differ in chromatographic behaviour, enzyme activating capacity, and slightly higher molecular mass (Mr = 12,500) from the major thioredoxin(s) present in mitochondria-free fractions of the same tissue. Both mt-thioredoxins can serve as hydrogen donor for E. coli ribonucleotide reductase but only the plant protein activates spinach chloroplast NADP malate dehydrogenase in vitro. Mitochondrial target enzymes specifically activated by thioredoxin have not as yet been identified.
硫氧还蛋白已从猪心和马铃薯块茎线粒体中纯化出来，它们在色谱行为、酶激活能力方面存在差异，并且分子量（Mr = 12,500）略高于同一组织无线粒体部分中存在的主要硫氧还蛋白。两种线粒体硫氧还蛋白都可以作为大肠杆菌核糖核苷酸还原酶的氢供体，但只有植物蛋白能在体外激活菠菜叶绿体NADP苹果酸脱氢酶。尚未鉴定出被硫氧还蛋白特异性激活的线粒体靶酶。
