[Isolation and identification of N-terminal fragments of the A-alpha chain of bovine fibrinogen]

Ukr Biokhim Zh (1978). 1991 Mar-Apr;63(2):3-8.
[Article in Russian]

Abstract

A method is suggested to obtain and purify N-end fragments of A alpha-chain from bovine fibrinogen. To identify the N-end chain fragments the fluorescent properties of tryptophan and tyrosine composing them as well as hydrolysis by ancistron H, a thrombin-like enzyme of the snake venom, have been used for the first time.

Publication types

  • English Abstract

MeSH terms

  • Animals
  • Cattle
  • Chromatography, Liquid
  • Fibrinogen / chemistry
  • Fibrinogen / isolation & purification*
  • Fibrinopeptide A / metabolism
  • Fibrinopeptide B / metabolism
  • Hydrolysis
  • Serine Endopeptidases / chemistry
  • Snake Venoms
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet
  • Tryptophan / metabolism
  • Tyrosine / metabolism

Substances

  • Snake Venoms
  • Fibrinopeptide A
  • Fibrinopeptide B
  • Tyrosine
  • Tryptophan
  • Fibrinogen
  • Serine Endopeptidases
  • ancistron N