Relation of detergent HLB number to solubilization and stabilization of D-alanine carboxypeptidase from Bacillus subtilis membranes.
نویسندگان
چکیده
The ability of various nonionic detergents to solubilize D-alanine carboxypeptidase and other membrane-bound enzymes was correlated to a physical property of the detergent, the HLB number. Only a fairly narrow range of detergents were effective solubilizing agents. Purified carboxypeptidase required either a detergent or detergent plus a lipid fraction for stability. Only those detergents effective in solubilizing the enzyme were effective in stabilizing it.
منابع مشابه
D=Alanine Carboxypeptidase from Bacillus subtilis Membranes
The D-alanine carboxypeptidase was solubilized from the membranes of Bacillus subtilis with the nonionic detergent, Triton X-100, and pursed to homogeneity. The purified protein bound irreversibly radioactivity from [Wlpenicillin G. It contained a single polypeptide chain of molecular weight 50,000 and existed in solution as a protein-detergent aggregate of molecular weight about 350,000. The a...
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Seven or eight penicillin-binding proteins (PBPs) were detected in Bacillus subtilis membranes. By introducing covalent affinity chromatography employing cephalosporins as ligands, milligram amounts of three high molecular weight PBPs (PBP 1 ab, Mr = 120,000; PBP 2b, Mr = 94,000; and PBP 4, Mr = 78,000) were obtained without any contamination of the major PBP 5, the D-alanine carboxypeptidase. ...
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The D-alanine carboxypeptidase of Bacillus subtilis is a particulate enzyme that is irreversibly inactivated by penicillins and cephalosporins. However, the lethal concentrations of these antibiotics are not the same as those that inhibit enzymatic activity in vitro. 6-Aminopenicillanic acid inactivates at least 95% of the enzyme at nonlethal concentrations. Conversely, cephalothin is lethal at...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 70 10 شماره
صفحات -
تاریخ انتشار 1973