Isolation and partial characterization of a type II Fc receptor from a group A streptococcus.
Mol Cell Biochem
; 70(1): 57-66, 1986 Apr.
Article
em En
| MEDLINE
| ID: mdl-3520293
ABSTRACT
A group A streptococcal strain rich in Fc receptors was selected by an immunoblotting technique and used as the source for isolation of a functionally active Fc receptor. A variety of extraction techniques were compared including (1) heat extraction at neutral, acid or alkaline pH, (2) treatment with the enzymes mutanolysin, hyaluronidase, trypsin, papain or phage lysin, or (3) autoclaving or heating in the presence of sodium dodecyl sulfate. The most homogeneous receptor was recovered following heat extraction and contained two molecular weight forms. The major form had a molecular weight of 56 000 daltons and the minor form had a molecular weight of 38 000 daltons. These two proteins could be isolated without loss of activity by binding to and elution from a column of immobilized human IgG. An antibody prepared against a single form of the affinity purified receptor demonstrated reactivity with both molecular weight forms of the heat extracted receptor. The group A receptor was found to be both antigenically and physicochemically distinct from either the type I receptor found on the majority of Staphylococcus aureus strains or the type III Fc receptors found on the majority of group C streptococcal strains.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Streptococcus pyogenes
/
Receptores Fc
Idioma:
En
Revista:
Mol Cell Biochem
Ano de publicação:
1986
Tipo de documento:
Article