More similarity between bakers' yeast L-(+)-lactate dehydrogenase and liver microsomal cytochrome b5 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1975-05

AUTHORS

BEA GUIA, FLORENCE LEDERER, C. JACQ

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). More... »

PAGES

422-423

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/255422a0

DOI

http://dx.doi.org/10.1038/255422a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030111382

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/165435


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