Structural analysis of human platelet membrane glycoprotein I complex.

Abstract:

:The glycoprotein I complex, consisting of two polypeptides of Mr 210,000 and 150,000, was isolated from human platelet membranes by wheat germ lectin affinity chromatography. Glycocalicin, a soluble loosely bound membrane glycoprotein of Mr 150,000 related to the glycoprotein I system, was also purified. The isolated polypeptides were radioiodinated in sodium dodecyl sulfate/polyacrylamide gels and digested with trypsin, and the labeled peptide digest was analyzed by two-dimensional high-voltage electrophoresis and thin-layer chromatography. The two polypeptides of Mr 210,000 and 150,000 in the glycoprotein I complex had essentially identical radioactive peptide maps. Glycocalicin had a completely different tryptic peptide map. These studies shed light on the molecular relationships of some of the components of the platelet membrane glycoprotein I system. The possibility is raised that the receptorlike function of the intrinsic platelet membrane glycoproteins may be related to the polymeric subunit associations of the constituent polypeptides.

authors

Nachman RL,Kinoshita T,Ferris B

doi

10.1073/pnas.76.6.2952

subject

Has Abstract

pub_date

1979-06-01 00:00:00

pages

2952-4

issue

6

eissn

0027-8424

issn

1091-6490

journal_volume

76

pub_type

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