[Isolation and characteristics of surface proteins from Streptococcus group A]

Autor: E P, Savel'ev, E I, Blinnikova, S A, Bitko, O P, Degtiareva
Rok vydání: 1987
Předmět:
Zdroj: Biokhimiia (Moscow, Russia). 52(11)
ISSN: 0320-9725
Popis: Cell wall surface proteins of group A Streptococcus type 29 were extracted with 1 M hydroxylamine pH 6.0. The purification procedure included fractionation with ammonium sulfate and gel filtration on Sephadex G-150. SDS polyacrylamide gel electrophoresis revealed a number of proteins (approximately 20) with molecular mass of 70 kD; the difference in Mr between the proteins was 5-10 kD. Isoelectrofocusing demonstrated that the proteins are either acid (pI = 3.7) or weakly alkaline (pI = 7.7). Possible reasons for the heterogeneity of Streptococcus cell wall surface proteins are discussed.
Databáze: OpenAIRE