Abstract
vWF is one of the largest proteins in the body, both as a single subunit and certainly as a multimeric series. Recent advances in amino acid sequencing and molecular cloning have given insight into its composition. Functional studies have shown that the essential information for the function of vWF is present in its subunit 270-kd chain. Studies with proteolytic fragments using binding assays and specific MAbs have begun to unravel the relationship between the structure and function of this highly complex adhesive protein. At least five separate binding domains have been identified, of which four have been localized to some extent. A rapid increase in understanding this intriguing protein may be expected in the near future.
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CITATION STYLE
Girma, J. P., Meyer, D., Verweij, C. L., Pannekoek, H., & Sixma, J. J. (1987). Structure-function relationship of human von Willebrand factor. Blood. https://doi.org/10.1182/blood.v70.3.605.605
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