Isolation and some properties of an IgG Fc-binding protein from group A streptococci type 15

• An IgG Fc-binding protein was isolated from alkaline extracts of group A streptococci type 15 by ion-exchange chromatography and immunosorption on an IgG column. Ample use of protease inhibitors was necessary to achieve successful isolation. 600 micrograms protein was obtained from 60 g bacteria (wet weight). The protein appeared homogeneous on agarose gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 29,500. It contained appreciable amounts of the amino acids glutamic acid, alanine, leucine, aspartic acid and lysine, but little or no tyrosine, phenylalanine, proline, glucosamine or galactosamine. It precipitated human monoclonal IgG of all four sub-classes in agarose gels as well as polyclonal IgG, IgG Fc and normal human serum. It did not precipitate IgG Fab, IgA, IgM, IgD or free kappa or lambda chains.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Nyckelord

Amino Acids

Antigens, Bacterial

Bacterial Outer Membrane Proteins

Bacterial Proteins/immunology

Binding Sites, Antibody

Carrier Proteins

Chemical Phenomena

Chemical Precipitation

Chemistry, Physical

Chromatography, DEAE-Cellulose

Electrophoresis, Polyacrylamide Gel

Humans

Immunodiffusion

Molecular Weight

Receptors, Fc

Receptors, IgG

Receptors, Immunologic

Streptococcus pyogenes/metabolism

Publikations- och innehållstyp

art (ämneskategori)

ref (ämneskategori)