Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

Protein S is a cofactor of activated protein C; together they function as a regulator of blood coagulation. A human liver cDNA library constructed in bacteriophage lambda gt11 was screened with DNA fragments from a full-length bovine cDNA clone encoding protein S. Several cDNA clones were isolated and sequenced. The combined cDNA sequences encoded the mature protein and 15 residues of the leader sequence when compared to bovine protein S. Human protein S is a single-chain protein consisting of 635 amino acids with 82% homology to bovine protein S. After an NH2-terminal gamma-carboxyglutamic acid-containing region, there is a short region with thrombin-sensitive bond(s), followed by a region with four repeat sequences that are homologous to the precursor of mouse epidermal growth factor. In contrast to the other vitamin K-dependent plasma proteins, the COOH-terminal portion of human protein S does not show any resemblance to serine proteases.

Detaljer

Författare
  • Åke Lundwall
  • W. Dackowski
  • E. Cohen
  • M. Shaffer
  • A. Mahr
  • B. Dahlback
  • J. Stenflo
  • R. Wydro
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Läkemedelskemi

Nyckelord

Originalspråkengelska
Sidor (från-till)6716-20
TidskriftProc Natl Acad Sci U S A
Volym83
Utgåva nummer18
StatusPublished - 1986
PublikationskategoriForskning
Peer review utfördJa