title: Two-dimensional analysis of the structure of human von Willebrand factor.
abstract: Human von Willebrand factor (vWF) is synthesized as an extra large polymer; then, it is converted to lower molecular weight plasma multimers, originally composed of intact 225-kDa subunits, by a metalloproteinase. Proteolysis generates two fragments of 140-and 176-kDa, which originate from cleavage of peptide bond Tyr842-Met843 and which represent vWF residues 1-842 and 843-2050, respectively; a very small amount of 189-kDa fragment can also be found in normal plasma. We describe here a two-dimensional (2-D) method to analyze plasma vWF structure.
authors.forename: P
authors.initials: P
authors.lastname: Perutelli
authors.forename: S
authors.initials: S
authors.lastname: Catellani
authors.forename: P G
authors.initials: PG
authors.lastname: Mori
mesh_terms: D001704:Biopolymers; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D008970:Molecular Weight; D011487:Protein Conformation; D014841:von Willebrand Factor / Q000737:chemistry*
chemical_list: D001704:Biopolymers; D014841:von Willebrand Factor