Purification and partial characterization of CD9 antigen of human platelets.
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.
Higashihara
M
M
First Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
Takahata
K
K
Yatomi
Y
Y
Nakahara
K
K
Kurokawa
K
K
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology; D015703:Antigens, CD / Q000302:isolation & purification*; D000943:Antigens, Differentiation / Q000302:isolation & purification*; D001792:Blood Platelets / Q000276:immunology*; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D060245:Tetraspanin 29
D000906:Antibodies; D015703:Antigens, CD; D000943:Antigens, Differentiation; C554869:CD9 protein, human; D008562:Membrane Glycoproteins; D060245:Tetraspanin 29