Abstract:
:Glycoprotein V (GPV) is a membrane-associated, 82 Kd platelet glycoprotein that is hydrolyzed during thrombin activation to yield 69 Kd fragment. We have developed a rapid and simple method for isolation of the protein from platelet extracts using a combination of gel permeation, anion-exchange, and lectin affinity chromatography. The partial amino acid sequence was determined by analysis of peptides generated by digestion of the S-carboxyamido-methylated protein with Achromobacter protease I or cyanogen bromide. The sequence shows a remarkable periodicity of leucine residues, which is homologous to the consensus sequence of a highly diversified protein super-family with a common repetitive module. Thrombin cleavage site was determined to be located at the C-terminal region of GPV by analysis of the products separated by sizing and reversed-phase high performance liquid chromatography. By lectin blot analysis, the existence of mucin-type carbohydrate chains was indicated, as well as the existence of asparagine-linked carbohydrate chains shown by the amino acid sequence analysis. From these data, we report a structural model of GPV that is analogous to glycoprotein Ib.
journal_name
Bloodjournal_title
Bloodauthors
Shimomura T,Fujimura K,Maehama S,Takemoto M,Oda K,Fujimoto T,Oyama R,Suzuki M,Ichihara-Tanaka K,Titani Ksubject
Has Abstract,Author List Incompletepub_date
1990-06-15 00:00:00pages
2349-56issue
12eissn
0006-4971issn
1528-0020journal_volume
75pub_type
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