PMID: 9531488Jun 11, 1998Paper

Triplet structure of human von Willebrand factor

The Biochemical Journal
B FischerF Dorner

Abstract

Human von Willebrand factor (hp-vWF) is a high-molecular- mass protein found in plasma as a series of multimers. It consists of subunits comprising 2050 amino acids linked by disulphide bonds into multimers of various size ranging in molecular mass up to greater than 10000kDa. Partial proteolysis at position Tyr842-Mer843 of the subunit [Dent et al. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6306-6310] by a vWF-specific protease [Furlan et al. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 7503-7507] results in the generation of an N-terminal and a C-terminal fragment and the appearance of hp-vWF triplet bands. It has been suggested [Furlan et al. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 7503-7507] that (i) the intermediate triplet band of the primary dimer represents a dimer of two C-terminal fragments, (ii) the slower migrating satellite band of the primary dimer represents an asymmetric structure composed of a mature subunit to which one N-terminal and one C-terminal fragment are linked by disulphide bonds, and (iii) the faster migrating satellite band of the primary dimer contains two N-terminal fragments. Here we used recombinant vWF (r-vWF) for structural analysis of hp-vWF multimers. r-vWF exhibited no proteolytic degradation an...Continue Reading

Citations

May 10, 2006·British Journal of Haematology·D J Bowen, P W Collins
Oct 17, 2009·Proteomics·Ingrid MillerElisabetta Gianazza
Jun 25, 2010·American Journal of Hematology·Marlies R Ledford-Kraemer
May 27, 2008·Biophysical Journal·Enrico Di StasioRaimondo De Cristofaro
Dec 17, 2014·Biologicals : Journal of the International Association of Biological Standardization·Christoph KannichtBirte Fuchs
Aug 5, 2017·Biological Chemistry·Elisabeth Schwarz
Dec 29, 2021·Critical Reviews in Clinical Laboratory Sciences·Neil S HarrisWilliam E Winter

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