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Article

Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor.

The Journal of biological chemistry - 15 Jan 1991

Leyte A, van Schijndel H B, Niehrs C, Huttner W B, Verbeet M P, Mertens K, van Mourik J A

Abstract excerpt

The acidic region of the Factor VIII light chain was studied with regard to structural requirements for the formation of a functional von Willebrand factor (vWF)-binding site. Factor VIII mutants lacking the B domain, with additional deletions and an amino acid replacement within the sequence 1649-1689 were constructed using site-directed mutagenesis and expressed in Cos-1 cells. These mutants, which were...

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PMID: 1898735

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Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor.PMID 1898735Read ↗

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Biological activity of recombinant factor VIII variants lacking the central B-domain and the heavy-chain sequence Lys713-Arg740: discordant in vitro and in vivo activity.Semantic proximity Read ↗

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A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2).Semantic proximity Read ↗

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Asymmetric processing of mutant factor X Arg386Cys reveals differences between intrinsic and extrinsic pathway activation.Semantic proximity Read ↗

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