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Purification and partial characterization of CD9 antigen of human platelets
Author(s) -
Higashihara Masaaki,
Takahata Kyoya,
Yatomi Yutaka,
Nakahara Kazuhiko,
Kurokawa Kiyoshi
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80265-k
Subject(s) - platelet , chemistry , disulfide bond , biochemistry , antigen , intramolecular force , peptide sequence , microbiology and biotechnology , yield (engineering) , stereochemistry , biology , immunology , gene , materials science , metallurgy
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.