Parallel characterization of bovine von Willebrand protein (factor VIII-associated protein) by light scattering and SDS gel electrophoresis.
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.
D000818:Animals; D000941:Antigens / Q000302:isolation & purification*; D002417:Cattle; D004587:Electrophoresis, Agar Gel; D005169:Factor VIII / Q000276:immunology* / Q000302:isolation & purification; D008027:Light; D008970:Molecular Weight; D012542:Scattering, Radiation; D014841:von Willebrand Factor / Q000302:isolation & purification*
D000941:Antigens; D014841:von Willebrand Factor; D005169:Factor VIII