Affinity of integrin alpha 1 beta 1 from liver sinusoidal membranes for type IV collagen.
Hepatic sinusoidal membranes isolated from adult rats were extracted with detergent and fractionated on a wheat germ agglutinin affinity column. Bound glycoproteins were eluted with N-acetyl glucosamine and chromatographed on a type IV collagen affinity column. Recovery of the bound fraction by EDTA and analysis by SDS-PAGE revealed two glycoproteins with apparent molecular weights of 180,000 and 117,000. These were identified immunologically by Western blotting as the alpha and beta subunits of integrin alpha 1 beta 1.
Stamatoglou
S C
SC
National Institute for Medical Research, London, UK.
Bawumia
S
S
Johansson
S
S
Forsberg
E
E
Hughes
R C
RC
D000818:Animals; D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D016023:Integrins / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism*; D038981:Receptors, Collagen
D016023:Integrins; D011956:Receptors, Cell Surface; D038981:Receptors, Collagen; D003094:Collagen