Epitope mapping of the von Willebrand factor subunit distinguishes fragments present in normal and type IIA von Willebrand disease from those generated by plasmin.
A small but consistent proportion of the von Willebrand factor (vWF) in normal plasma is composed of 189, 176, and 140 kD fragments cleaved from the 225 kD subunit. A monoclonal antibody map of vWF, based on the reactivity of individual antibodies with cyanogen bromide and tryptic fragments of known carboxy and/or amino termini, showed that in normal and IIA von Willebrand disease (vWD) plasmas the 140 kD fragment was derived from the amino-terminal region, whereas the 176 kD fragment was derived from the carboxy-terminal region of the subunit. In type IIA vWD, however, the fragments comprised a greater proportion of circulating vWF. In contrast, plasmin cleaved a 176 kD fragment from the amino terminus and a 145 kD fragment from the carboxy terminus of the subunit. Species similar to these plasmin-cleaved fragments were demonstrated in plasmas from four patients treated with fibrinolytic agents, but not in IIA vWD.
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Related Subject Headings
- von Willebrand Factor
- von Willebrand Diseases
- Peptide Fragments
- Molecular Weight
- Macromolecular Substances
- Immunology
- Humans
- Fibrinolysin
- Epitopes
- Antibodies, Monoclonal
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- von Willebrand Factor
- von Willebrand Diseases
- Peptide Fragments
- Molecular Weight
- Macromolecular Substances
- Immunology
- Humans
- Fibrinolysin
- Epitopes
- Antibodies, Monoclonal