Higashihara M, Takahata K, Yatomi Y, Nakahara K, Kurokawa K
First Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
FEBS Lett. 1990 May 21;264(2):270-4. doi: 10.1016/0014-5793(90)80265-k.
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.
CD9抗原（p24）从人血小板中纯化并进行了部分特性鉴定。从10单位血小板浓缩物中获得的产量为75微克。p24（每个血小板38,000个拷贝）具有分子内二硫键，在SDS-PAGE中由主要的24 kDa分子和次要的26至31 kDa分子组成。p24的N端序列PVKGGTKXIKYLLFGFNFIF表明该蛋白质以前未被鉴定过，且氨基末端（第12 - 20位）具有疏水性。
