Peripheral and integral proteins of human blood platelet membranes. alpha-Actinin is not identical to glycoprotein III.
Isolation of human platelet membranes on polylysine beads and selective solubilization of membrane proteins allowed classification of membrane-associated proteins into integral and peripheral proteins. No major integral protein was found that was not exposed on the surface. Glycoprotein Ic was the only surface-exposed protein that behaved as a peripheral protein. The localization and identification of alpha-actinin was performed with an antibody against porcine skeletal muscle alpha-actinin. Human platelet alpha-actinin had an apparent molecular weight of 100 000 and a pI of 5.7-6.3. It was membrane-associated and behaved as a peripheral protein. Immunoisolation on protein A beads, as well as the 'Western Blot' technique applied to two-dimensional gels, demonstrated that alpha-actinin is not identical to GP III as was previously suggested (Gerrard, J.M., Schollmeyer, J.V., Phillips, D.R. and White, J.G. (1979) Am. J. Pathol. 94, 509-528).
D000185:Actinin / Q000032:analysis* / Q000097:blood; D001792:Blood Platelets / Q000032:analysis*; D002458:Cell Fractionation / Q000379:methods; D002462:Cell Membrane / Q000032:analysis; D006023:Glycoproteins / Q000097:blood*; D006801:Humans; D007526:Isoelectric Point; D008565:Membrane Proteins / Q000097:blood; D009124:Muscle Proteins / Q000032:analysis*; D012995:Solubility
D006023:Glycoproteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D000185:Actinin