Abstract
BAKERS' yeast L-lactate dehydrogenase, or cytochrome b2 (EC 1.1.2.3.), catalyses the oxidation of L-(+)-lactate to pyruvate. When purified in the presence of phenylmethane-sulphonylfluoride, it is a tetramer of four presumably identical polypeptide chains of molecular weight 57,000, each of which carries one flavin mononucleotide and one protohaem IX (ref. 1). In the absence of protease inhibitor, the enzyme obtained by the classical crystallisation method of Appleby and Morton2 shows cleavages at the N terminus and at a region about two-thirds down the chain, in each monomer; it is then composed of four chains (α) of molecular weight about 36,000 and four chains (β) of about 21,000 (ref. 1).
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GUIARD, B., LEDERER, F. & JACQ, C. More similarity between bakers' yeast L-(+)-lactate dehydrogenase and liver microsomal cytochrome b5. Nature 255, 422–423 (1975). https://doi.org/10.1038/255422a0
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DOI: https://doi.org/10.1038/255422a0
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