Intact bacterial membranes have been isolated from protoplasts prepared from Group A streptococci by a cell wall-dissolving enzyme. A membrane fraction with identical chemical and serological properties has been obtained by differential centrifugation of mechanically disrupted streptococci. The membrane is chemically distinct from the cell wall and is composed of 72 per cent protein, 26 per cent lipid, and 2 per cent carbohydrate. Capillary precipitin tests and analysis by microdiffusion have demonstrated that the membrane contains antigens distinct from those of the cell wall and from those of the cytoplasm which it envelops. Evidence is presented which demonstrates that this antigenic material is common to the membranes of Group A streptococci, and that it can be distinguished by immunodiffusion from related antigenic substances present in membranes of several other serological groups of hemolytic streptococci. This antigenic material does not cross-react with the membrane antigens of other Gram-positive cocci.
Skip Nav Destination
Article navigation
1 March 1963
Article|
March 01 1963
STUDIES OF L FORMS AND PROTOPLASTS OF GROUP A STREPTOCOCCI : II. CHEMICAL AND IMMUNOLOGICAL PROPERTIES OF THE CELL MEMBRANE
Earl H. Freimer
Earl H. Freimer
From The Rockefeller Institute
Search for other works by this author on:
Earl H. Freimer
From The Rockefeller Institute
Received:
October 17 1962
Online ISSN: 1540-9538
Print ISSN: 0022-1007
Copyright ©, 1963, by The Rockefeller Institute
1963
J Exp Med (1963) 117 (3): 377–399.
Article history
Received:
October 17 1962
Citation
Earl H. Freimer; STUDIES OF L FORMS AND PROTOPLASTS OF GROUP A STREPTOCOCCI : II. CHEMICAL AND IMMUNOLOGICAL PROPERTIES OF THE CELL MEMBRANE . J Exp Med 1 March 1963; 117 (3): 377–399. doi: https://doi.org/10.1084/jem.117.3.377
Download citation file:
Sign in
Don't already have an account? Register
Client Account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your Institution
Sign in via your InstitutionSuggested Content
Email alerts
Advertisement