title: Isolation of a fibronectin-binding tryptic peptide from the antigen 85A protein of Mycobacterium bovis BCG.
abstract: Antigen 85A, a major secreted mycobacterial fibronectin-binding protein, was isolated from culture fluids of the Tice substrain BCG vaccine. Tryptic digestion of this protein and passage of the digest through a fibronectin affinity chromatographic column resulted in the identification of a polypeptide fragment of molecular weight < or = 6.5 kD, which had marked fibronectin-binding activity. The identity of a 62-residue polypeptide was deduced from the amino-terminal sequence, indicating that the primary structure may define the integrin-binding capability.
authors.affiliation: Institute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago 60607.
authors.forename: M E
authors.initials: ME
authors.lastname: Klegerman
authors.forename: F
authors.initials: F
authors.lastname: Oner
authors.forename: P
authors.initials: P
authors.lastname: Morris
authors.forename: K
authors.initials: K
authors.lastname: Son
authors.forename: M J
authors.initials: MJ
authors.lastname: Groves
mesh_terms: D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000378:metabolism*; D015153:Blotting, Western; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009163:Mycobacterium bovis / Q000737:chemistry* / Q000276:immunology; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D014357:Trypsin
chemical_list: D000942:Antigens, Bacterial; D010455:Peptides; C065036:antigen 85, Mycobacterium bovis; D005340:Fibrinogen; D014357:Trypsin