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. 1986 Feb;12(2):207-14.

Characterization of beta-lactamase from Mycobacterium butyricum ATCC 19979

  • PMID: 3485977

Characterization of beta-lactamase from Mycobacterium butyricum ATCC 19979

D Choubey et al. Biochem Int. 1986 Feb.

Abstract

beta-lactamase has been purified to a homogeneous state from Mycobacterium butyricum ATCC 19979. The molecular weight (Mr = 29,000) and the isoelectric point (4,0) of the enzyme have been determined. The enzyme showed both penicillinase and cephalosporinase activity, but had relatively more of the former. With respect to substrate-profile the enzyme resembled the plasmid specified TEM-type beta-lactamases commonly encountered in Gram-negative bacteria. The enzyme was insensitive to p-chloromercuribenzoate, sodium chloride, or iodine inhibition.

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