Studies on phosphoglyceromutase from chicken breast muscle: number and reactivity of sulfhydryl groups

Carne, T.J.; McKay, D.J.; Flynn, T.G.

Canadian Journal of Biochemistry 54(4): 307-320

1976


ISSN/ISBN: 0008-4018
PMID: 178418
DOI: 10.1139/o76-046
Accession: 068523152

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Abstract
Phosphoglyceromutase (PGM) from chicken breast muscle was titrated with p-mercuribenzoate (PMB), 5,5'-dithiobisnitrobenzoate (Nbs2), N-ethylmaleimide (NEM), iodoacetate and iodoacetamide. The effect of all of the sulfhydryl reagents, with the exception of NEM was to cause a loss in enzymatic activity. Addition of KCN following reaction with Nbs2 resulted in the recovery of a small amount of enzymatic activity. In the absence of substrate (3-phosphoglyceric acid) or cofactor (2,3-diphosphoglyceric acid) and in the presence or absence of 6 M guanidine hydrochloride, six sulfhydryl groups per mole of enzyme were titrated with PMB.