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  • Title: Identification of PlAl alloantigen domain on a 66 kDa protein derived from glycoprotein IIIa of human platelets.
    Author: Kornecki E, Chung SY, Holt JC, Cierniewski CS, Tuszynski GP, Niewiarowski S.
    Journal: Biochim Biophys Acta; 1985 Sep 10; 818(3):285-90. PubMed ID: 2994725.
    Abstract:
    Incubation of platelets with chymotryptin leads to the exposure of fibrinogen receptors and to the appearance of a 66 kDa membrane component on the surface of platelets. Both glycoprotein IIIa (GP IIIa) and a 66 kDa component were precipitated from detergent extracts of solubilized, surface radiolabeled chymotrypsin-treated platelets by human anti-PlAl antisera. Moreover, the presence of the P1A1 antigen was identified on GP IIIa (but not on GP IIb) and on a 66 kDa protein by means of immunoblot procedures using platelet Triton X-114 extracts and these purified proteins. Anti-PlAl antiserum did not recognize GP IIIa on the surface of intact (untreated) platelets nor the 66 kDa protein on the surface of chymotrypsin-treated platelets of PlAl-negative individuals. The present data demonstrate directly that the 66 kDa protein is derived from GP IIIa and contains the PlAl alloantigen.
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