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Published on: December 27, 2017
Purification and partial characterization of CD9 antigen of human platelets
M Higashihara1, K Takahata, Y Yatomi
1First Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
Abstract:
CD9 antigen (p24) was purified from human platelets and partially characterized. The yield was 75 micrograms from 10 units of platelet concentrates. p24 (38,000 copies/platelet) has intramolecular disulfide bond(s) and, in SDS-PAGE, consists of major 24-kDa molecule and minor 26- to 31-kDa molecules. The N-terminal sequence of p24, PVKGGTKXIKYLLFGFNFIF, indicates that the protein has not previously been characterized and amino terminus (position 12-20) is hydrophobic.
