Determination of the disulphide bridge arrangement of bovine histidine-rich glycoprotein

FEBS Lett. 1993 Aug 16;328(3):285-90. doi: 10.1016/0014-5793(93)80945-q.

Abstract

Histidine-rich glycoprotein (HRG) was purified from bovine plasma and the disulphide bridge arrangement established. Disulphide-bridged peptides were obtained from peptic and tryptic degradation of native bovine HRG. Twelve half-cystine residues were found in bovine HRG (compared to sixteen cysteines in human HRG), all involved in the formation of six disulphide bridges connecting Cys-1 to Cys-12, Cys-2 to Cys-3, Cys-4 to Cys-5, Cys-6 to Cys-11, Cys-7 to Cys-8, and Cys-9 to Cys-10. Additional sequence analysis of 14C-carboxymethylated chymotryptic and Staphylococcus aureus V8 protease generated peptides and CNBr-fragments of bovine HRG yielded a partial amino acid sequence of bovine HRG constituting 78% of the sequence when compared to the human cDNA sequence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Asparagine / chemistry
  • Cattle
  • Cysteine / analysis
  • Disulfides / chemistry*
  • Glycoproteins / analysis*
  • Humans
  • Molecular Sequence Data
  • Polymorphism, Genetic
  • Proteins / analysis*
  • Sequence Homology, Amino Acid

Substances

  • Disulfides
  • Glycoproteins
  • Proteins
  • histidine-rich proteins
  • Asparagine
  • Cysteine