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

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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 164...

Topics

Binding, Competitive
Culture Techniques
DNA
Factor VIII
Humans
Methionine
Mutation
Plasmids
Sulfuric Acids
Transfection
Tyrosine
von Willebrand Factor

Source

Open in PubMed

Identifiers

PMID: 1898735

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1898735-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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