title: [Isolation of the fifth IgG-binding domain from Staphylococcus aureus protein A].
abstract: Using affinity chromatography on IgG-Sepharose at pH 5.0, a new fragment capable of binding to IgG (domain E) was isolated from trypsin hydrolysate of protein A. Trypsinolysis of protein A was performed at low temperatures. Thus, the intact structure of protein A was found to include six domains, of which five interact with IgG.
authors.forename: V M
authors.initials: VM
authors.lastname: Tishchenko
authors.forename: V I
authors.initials: VI
authors.lastname: Surovtsev
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002846:Chromatography, Affinity; D006868:Hydrolysis; D007074:Immunoglobulin G / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification*; D013205:Staphylococcal Protein A / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D007074:Immunoglobulin G; D010446:Peptide Fragments; D013205:Staphylococcal Protein A
vernacular_title: Vydelenie piatogo IgG-sviazyvaiushchego domena iz belka A Staphylococcus aureus]