Abstract
Diisopropyl fluorophosphate (DFP) effectively inhibited proteolytic activity in preparations of partially purified Streptomyces albus enzyme used to lyse cell walls of Group A streptococci. Lysis of non-trypsinized Group A cell walls with DFP-treated S. albus enzyme released 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. The similarities of the products of DFP-treated S. albus enzyme lysis of streptococcal cell walls to those released by phage muralytic enzyme furnish additional evidence of the close relationship of these wall lysins. In view of small differences in electrophoretic 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.
Keywords
BACTERIOLYSIS
CHEMISTRY
CHEMISTRY
ANALYTICAL
CHROMATOGRAPHY
ELECTROPHORESIS
ENZYMES
EXPERIMENTAL LAB STUDY
IMMUNOELECTROPHORESIS
ISOFLUROPHATE
PHARMACOLOGY
POLYSACCHARIDES
BACTERIAL
STREPTOCOCCUS
MeSH Terms
Bacteriolysis
Cell Wall
Chemical Phenomena
Chemistry
Chemistry Techniques, Analytical
Chromatography
Electrophoresis
Enzymes
Fluorides
Immunoelectrophoresis
Isoflurophate
Pharmacology
Phosphates
Polysaccharides, Bacterial
Research
Streptococcus
Streptococcus pyogenes
Streptomyces
Chemicals
Enzymes
Phosphates
Polysaccharides, Bacterial
streptococcal polysaccharide group A
Isoflurophate
fluorophosphate
Fluorides
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
SCHMIDT W C
References (22)
22 references, click to expand
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