THE LYSIS OF CELL WALLS OF GROUP A STREPTOCOCCI BY STREPTOMYCES ALBUS ENZYME TREATED WITH DIISOPROPYL FLUOROPHOSPHATE

Open Access
Publisher Website
Google Scholar
Abstract
Non-trypsinizedcell walls of Group A streptococci were lysed by Streptomyces albus enzyme treated with diisopropyl fluorophosphate (DFP) to inhibit traces of proteolytic enzyme present in the partially purified preparations of enzyme. A soluble protein fraction containing antigenic type-specific M protein, a carbohydrate fraction consisting of Group A and a small amount of A variant polysaccharides, and a dialyzable fraction composed principally of serologically inactive cell wall mucopeptide fragments were released. The products of DFP-treated S. albus enzyme lysis of streptococcal cell walls closely resemble comparable components of phage-associated enzyme lysates of trypsinized streptococcal walls. However, additional amino acids were present in the dialyzable mucopeptide and mucopeptide conjugated to polysaccharide from S. albus lysates of whole walls. In view of small differences in electro-phoretic mobility, immunodiffusion and chemical composition, it is suggested that Group A streptococcal cell wall polysaccharide dissolved by DFP-S. albus enzyme consists of a spectrum of molecules having the same immunological determinants but differing in content of conjugated mucopeptide.