[Isolation and characteristics of surface proteins from Streptococcus group A].
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.
Savel'ev
E P
EP
Blinnikova
E I
EI
Bitko
S A
SA
Degtiareva
O P
OP
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002473:Cell Wall / Q000032:analysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D013297:Streptococcus pyogenes / Q000032:analysis*
D000596:Amino Acids; D001426:Bacterial Proteins; D010455:Peptides
Vydelenie i kharakteristika poverkhnostnykh belkov streptokokka gruppy A.