Characterization of clinical isolates of group C and G streptococci on the basis of protein G gene.
Treatment of human group C and G streptococci with cyanogen bromide results in solubilization of surface protein G molecules. Strain-to-strain variation in the quantity, molar mass and functional activity of protein G extracted from representative group C and G isolates led to the identification of three structurally and functionally distinct forms of the protein. Using different molecular biological approaches it was possible to determine the group of streptococci (C or G), or the quantity of IgG and HSA domains.
Gupalova
T
T
Institute of Experimental Medicine, St. Petersburg, Russia.
Voltchek
N
N
Totolyan
A
A
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D066298:In Vitro Techniques; D008970:Molecular Weight; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism; D013290:Streptococcal Infections / Q000382:microbiology*; D013291:Streptococcus / Q000145:classification* / Q000235:genetics* / Q000302:isolation & purification
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D007074:Immunoglobulin G; D012709:Serum Albumin