Animal and plant mitochondria contain specific thioredoxins

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Abstract
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.