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Appl Environ Microbiol. 1971 December; 22(6): 963-973
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Evaluation of Methods Used to Purify Acid-Extracted Group A Streptococcal M Protein

Center for Disease Control, Atlanta, Georgia 30333

ABSTRACT

The literature includes descriptions of both acid-soluble and acid-insoluble M protein in the preparation of "hot acid-extracted group A streptococcal M protein." We present evidence for the contamination of crude type 1 acid-insoluble M protein. The purification of preparations of crude and partially purified acid-soluble type 1 and type 12 M protein is described. Our quantitative criteria for purification were recovery of M precipitin activity, improvement in specific activity, and removal of carbohydrate. Exclusion of nucleic acid is also discussed. Greater purification in a single passage was found with a carboxymethylcellulose column (with acidic elution) than with hydroxyapatite, diethylaminoethyl-Sephadex, or carboxymethyl-cellulose (with neutral elution) columns or with ammonium sulfate fractional precipitation. Carboxymethylcellulose with acidic elution was found to be a satisfactory standard laboratory procedure for the preparation of purified acid-extracted (acid-soluble) group A streptococcal M protein.

¹ Present address: Department of Endocrinology and Metabolism, Barnes & Whol Hospitals, St. Louis, Mo. 63110.