| Autor: |
Hiraiwa, Akikazu, Matsukage, Akio, Shiku, Hiroshi, Takahashi, Toshitada, Naito, Kazuyuki, Yamada, Kazumasa |
| Zdroj: |
Blood; February 1987, Vol. 69 Issue: 2 p560-564, 5p |
| Abstrakt: |
The glycoprotein (GP) llb—llla complex was isolated from human platelet membranes by immunoaffinity chromatography using a monoclonal antibody specific for GP llb—Illa. GP llb and llla were further separated in the presence of sodium dodecyl sulfate (SDS) by gel filtration high-perfor-mance liquid chromatography (HPLC). Two cycles of this procedure yielded almost complete separation of homogeneous preparations of GP lib and llla. Each protein was then digested with lysyl endopeptidase (Achromobacterprotease I), which cleaves at the carboxyl side of lysine residues, and the resulting oligopeptides from GP llb and llla were fractionated with HPLC using a C18 reverse-phase column. Comparison of the elution profiles showed no obvious homology between the two proteins. Amino acid sequences of selected oligopeptides from each glycoprotein were determined using a gas-phase protein sequencer. Sixty amino acid residues (26 residues for llb and 34 residues for llla) were identified. © 1987 by Grune & Stratton, Inc. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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