PURIFICATION AND PARTIAL CHARACTERIZATION OF CD9 ANTIGEN OF HUMAN PLATELETS

被引：20

作者：

HIGASHIHARA, M ^{[1
]}

TAKAHATA, K ^{[1
]}

YATOMI, Y ^{[1
]}

NAKAHARA, K ^{[1
]}

KUROKAWA, K ^{[1
]}

机构：

[1] KUREHA CHEM IND CO LTD, SHINJUKU KU, TOKYO 160, JAPAN

来源：

FEBS LETTERS | 1990年 / 264卷 / 02期

关键词：

CD9; N-terminal sequence; Platelet;

D O I：

10.1016/0014-5793(90)80265-K

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CD9 antigen (p24) was purified from human platelets and partially characterized. The yield was 75 μg 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, PVKGOTKXIKYLLFGFNFIF, indicates that the protein has not previously been characterized and amino terminus (position 12-20) is hydrophobic. © 1990.

引用

页码：270 / 274

页数：5

共 34 条

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