Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa.

Abstract:

:The glycoprotein (GP) IIb-IIIa complex was isolated from human platelet membranes by immunoaffinity chromatography using a monoclonal antibody specific for GP IIb-IIIa. GP IIb and IIIa were further separated in the presence of sodium dodecyl sulfate (SDS) by gel filtration high-performance liquid chromatography (HPLC). Two cycles of this procedure yielded almost complete separation of homogeneous preparations of GP IIb and IIIa. Each protein was then digested with lysyl endopeptidase (Achromobacter protease I), which cleaves at the carboxyl side of lysine residues, and the resulting oligopeptides from GP IIb and IIIa 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 IIb and 34 residues for IIIa) were identified.

journal_name

Blood

journal_title

Blood

authors

Hiraiwa A,Matsukage A,Shiku H,Takahashi T,Naito K,Yamada K

subject

Has Abstract

pub_date

1987-02-01 00:00:00

pages

560-4

issue

2

eissn

0006-4971

issn

1528-0020

journal_volume

69

pub_type

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