Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)

J Biol Chem. 1985 May 10;260(9):5328-41.

Abstract

The amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor) was determined by automated Edman degradation using the peptides produced by chemical and enzymatic cleavages of intact factor XII and alpha-factor XIIa. Combining this sequence with the previously determined sequence of beta-factor XIIa (Fujikawa, K., and McMullen, B. A. (1983) J. Biol. Chem. 258, 10924-10933), the complete amino acid sequence of human factor XII has been established. The heavy chain of alpha-factor XIIa is composed of 353 amino acid residues containing one Asn-linked and six probable O-linked carbohydrate chains. The heavy chain of alpha-factor XIIa appears to contain four different domains including a "kringle," a "growth factor" domain, and the "type I" and "type II" domains of fibronectin. The domain organization of factor XII is analogous to those of several fibrinolytic proteins, including tissue plasminogen activator and urokinase, suggesting that factor XII belongs to the same protease subfamily as these two proteins.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Chymotrypsin / metabolism
  • Cyanogen Bromide / pharmacology
  • Endopeptidases / metabolism
  • Factor XII / analysis*
  • Factor XIIa
  • Humans
  • Peptide Fragments / analysis*
  • Protein Conformation
  • Serine Endopeptidases*
  • Trypsin / metabolism

Substances

  • Peptide Fragments
  • Factor XII
  • Endopeptidases
  • Serine Endopeptidases
  • Chymotrypsin
  • glutamyl endopeptidase
  • Factor XIIa
  • Trypsin
  • lysyl endopeptidase
  • Cyanogen Bromide