Abstract
The γ-type β-lactamase has been extracted from cells of Bacillus cereus strain 569 H and purified (135-fold) by selective adsorption on cellulose phosphate and by CM-cellulose chromatography. The enzyme was compared with the purified α-type β-lactamase obtained from the culture supernatant fraction of the same organism. The two enzymes show many similarities but differ in several properties, including substrate specificity, stability to heat and proteolysis, and susceptibility to conformation distorting effects of substrate analogs. The differences appear to be related to the postulated difference in the tertiary structure of the two types of β-lactamase.
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