Isolation of a fibronectin-binding tryptic peptide from the antigen 85A protein of Mycobacterium bovis BCG.
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.
Klegerman
M E
ME
Institute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago 60607.
Oner
F
F
Morris
P
P
Son
K
K
Groves
M J
MJ
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
D000942:Antigens, Bacterial; D010455:Peptides; C065036:antigen 85, Mycobacterium bovis; D005340:Fibrinogen; D014357:Trypsin