Parallel characterization of bovine von Willebrand protein (factor VIII-associated protein) by light scattering and SDS gel electrophoresis.

Abstract:

:Highly purified bovine von Willebrand protein (vWP) has been studied with two complementary techniques. Light scattering measurements on different samples give weight average molecular weights in the range from 7 to 13 million, radius of gyration between 75 and 140 nm and diffusion coefficient near 4.15 X 10(-8) cm2/sec. Scans after electrophoresis in sodium dodecyl sulfate on 2% agarose gels, stained with Coomassie blue, allow calculation of a mass distribution over a series of oligomers with relative size in a range from 1 to 20. The ratio of the average mol. wt. from light scattering and the average size for the observed distribution, which is the mol. wt. increment for successive vWP oligomers, has been determined and found to be 1.0 million. This implies that the molecules of vWP are oligomers of subunits themselves consisting of 4 polypeptide chains each of mol. wt. circa 250,000.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Binnie C,Wagner RH,Cooper H,Hermans J

doi

10.1016/0049-3848(85)90289-0

subject

Has Abstract

pub_date

1985-11-15 00:00:00

pages

523-32

issue

4

eissn

0049-3848

issn

1879-2472

journal_volume

40

pub_type

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