Identification and isolation of vinculin from platelets.
A vinculin-like protein was identified in chicken as well as in bovine platelets by ELISA competitive binding assay using antibodies against vinculin from chicken gizzard. By a modified procedure (J. Biol. Chem. (1980) 255, 1194-1199) we succeeded in isolating bovine platelet vinculin to apparent homogeneity. The structural identity of platelet and chicken gizzard vinculin was demonstrated by circular dichroism analysis. It was also shown that platelet vinculin induces a significant decrease in the low shear viscosity of F-actin. Vinculin, in all probability, plays an important role in the organization of actin filaments in platelets, especially in the linkages of microfilaments to the membrane.
D000199:Actins; D000818:Animals; D001667:Binding, Competitive; D001792:Blood Platelets / Q000032:analysis*; D002417:Cattle; D002645:Chickens / Q000097:blood; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D009124:Muscle Proteins / Q000097:blood* / Q000276:immunology / Q000494:pharmacology; D009130:Muscle, Smooth / Q000032:analysis; D011487:Protein Conformation; D016596:Vinculin; D014783:Viscosity
D000199:Actins; D000939:Epitopes; D009124:Muscle Proteins; D016596:Vinculin