Characterization of beta-lactamase from Mycobacterium butyricum ATCC 19979.
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.
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D007700:Kinetics; D008970:Molecular Weight; D009161:Mycobacterium / Q000201:enzymology*; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000302:isolation & purification* / Q000378:metabolism
D001618:beta-Lactamases