Production and Purification of the Extracellular Ribonuclease of Bacillus Amyloliquefaciens (Barnase) and its Intracellular Inhibitor (Barstar) II. Barstar

Robert W. Hartley Laboratory of Nutrition and Endocrinology National, Institute of Arthritis and Metabolic Diseases National Institutes of Health, Bethesda, Maryland, 20014; Applications Laboratory, Laboratory Medicine Department, The Perkin-Elmer Corporation, Norwalk, Connecticut

David L. Rogerson Jr. Laboratory of Nutrition and Endocrinology National, Institute of Arthritis and Metabolic Diseases National Institutes of Health, Bethesda, Maryland, 20014; Applications Laboratory, Laboratory Medicine Department, The Perkin-Elmer Corporation, Norwalk, Connecticut

John R. Smeaton Laboratory of Nutrition and Endocrinology National, Institute of Arthritis and Metabolic Diseases National Institutes of Health, Bethesda, Maryland, 20014; Applications Laboratory, Laboratory Medicine Department, The Perkin-Elmer Corporation, Norwalk, Connecticut

Abstract

Procedures are reported for the extraction and purification of barstar, the intracellular inhibitor of barnase, the extracellular ribonuclease of Bacillus amyloliquefaciens, (a strain formerly erroneously classified as B. subtilis, strain H), from frozen acidified cells obtained during the isolation of barnase¹. Methods include affinity chromatography on agarose to which barnase is covalently bound. Experiments relating to the purity, molecular weight, and amino acid composition of the product are reported.

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Production and Purification of the Extracellular Ribonuclease of Bacillus Amyloliquefaciens (Barnase) and its Intracellular Inhibitor (Barstar) II. Barstar

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Production and Purification of the Extracellular Ribonuclease of Bacillus Amyloliquefaciens (Barnase) and its Intracellular Inhibitor (Barstar) II. Barstar

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