Propolypeptide and mature portions of von Willebrand factor of bovine origin recognize different sites on type-I collagen obtained from bovine tendon.
We compared the binding of propolypeptide and mature portions of von Willebrand factor of bovine origin to fibrillar type-I collagen obtained from bovine tendon. The propolypeptide (pp-vWF) and the mature portion (m-vWF) of human origin consist of 741 and 2050 amino acids, respectively, and are rather large proteins. The collagen-binding properties of the two proteins of bovine origin were similar in that both bound more avidly to native collagen than to heat-denatured collagen. Bindings was affected similarly by ionic strength but was not modified either by divalent cations or a synthetic peptide containing Arg-Gly-Asp. However, the binding sites in the fibrillar type-I collagen molecule for pp-vWF and m-vWF seem to be different: the two proteins did not effectively compete with each other for binding to collagen. Furthermore, pepsin treatment of fibrillar type-I collagen resulted in a drastic decrease in the binding of pp-vWF, while only a moderate decrease in the binding of m-vWF was observed after the treatment.
Usui
T
T
Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Japan.
Fujisawa
T
T
Takagi
J
J
Saito
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002413:Cations, Divalent; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology; D009994:Osmolar Concentration; D010455:Peptides / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism*; D013379:Substrate Specificity; D013710:Tendons / Q000378:metabolism*; D014841:von Willebrand Factor / Q000378:metabolism*
D002413:Cations, Divalent; D009842:Oligopeptides; D010455:Peptides; D011498:Protein Precursors; D014841:von Willebrand Factor; D003094:Collagen