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  • Title: Association of a 24-kDa GTP-binding protein, Gn24, with human platelet alpha-granule membranes.
    Author: van der Meulen J, Bhullar RP, Chancellor-Maddison KA.
    Journal: FEBS Lett; 1991 Oct 07; 291(1):122-6. PubMed ID: 1936239.
    Abstract:
    Human platelets were disrupted using nitrogen cavitation and fractionated on sucrose density gradients to permit isolation of alpha-granules, the major secretory granule of platelets. Membrane proteins prepared from intact alpha-granules by alkali extraction were separated by SDS-polyacrylamide gel electrophoresis, transferred to nitrocellulose and the blot probed for the presence of GTP-binding proteins using [alpha-32P]GTP. Two low molecular mass GTP-binding proteins with molecular mass of 27 and 24 kDa, respectively, were identified on the alpha-granule membrane. In contrast to the 27-kDa protein which was present in significant amounts in the plasma membrane-enriched fraction, the 24-kDa protein showed a preferential association with the alpha-granule membrane. On immunoblotting with specific antiserum, the 24-kDa GTP-binding protein was found to be distinct from rab3A. To the best of our knowledge, the present report represents the first identification of low molecular mass GTP-binding proteins associated with a platelet secretory granule.
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