Purification and partial characterization of CD9 antigen of human platelets.
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Higashihara M, Takahata K, Yatomi Y, Nakahara K, Kurokawa K
Purification and partial characterization of CD9 antigen of human platelets.
FEBS Lett. 1990 May 21;264(2):270-4.
- PubMed ID
- 2358073 [ View in PubMed]
- 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.