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• W2006243432 endingPage "126" @default.
• W2006243432 startingPage "122" @default.
• W2006243432 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." @default.
• W2006243432 created "2016-06-24" @default.
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• W2006243432 date "1991-10-07" @default.
• W2006243432 modified "2023-09-23" @default.
• W2006243432 title "Association of a 24-kDa GTP-binding protein, Gn24, with human platelet α-granule membranes" @default.
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• W2006243432 doi "https://doi.org/10.1016/0014-5793(91)81118-r" @default.
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