Sequencing of the primary adhesion domain of bovine von Willebrand factor.
A cDNA library, constructed from bovine heart endothelial cell poly(A)+ RNA, was screened using a BstXI fragment of human von Willebrand and factor (vWF) cDNA as a probe. This probe codes for the major adhesion domain of vWF that includes the GPIb, collagen and heparin binding domains. Of the ten positive clones obtained, a clone that spanned the region of interest was sequenced by the dideoxynucleotide method yielding a sequence of 1550 bp. This region of the bovine cDNA codes for amino acids corresponding to #262 to #777 in human vWF and encompasses the entire pro adhesion domain. Both the nucleotide sequence and the deduced amino acid sequence are 82% homologous to those of human vWF. Cysteine residues #471, 474, 509 and 695, which form intrachain bonds in human vWF, are also present in the bovine vWF sequence.
Bakhshi
M R
MR
Department of Biochemistry, Temple University School of Medicine, Philadelphia, PA 19140.
Myers
J C
JC
Howard
P S
PS
Soprano
D R
DR
Kirby
E P
EP
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002448:Cell Adhesion / Q000235:genetics; D004247:DNA; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014841:von Willebrand Factor / Q000235:genetics*
D014841:von Willebrand Factor; D004247:DNA