[Isolation of protein of the chymotrypsin inhibitor from honey locust seeds]

Biokhimiia. 1982 Dec;47(12):2015-21.
[Article in Russian]

Abstract

The chymotrypsin inhibitor was isolated from honey locust (Gleditsia triacanthos L.) by chromatography on trypsin- and chymotrypsin-Sepharose 4B and by gel filtration on Sephadex G-75. The inhibitor can inhibit chymotrypsin but has no effect on trypsin, subtilisin and proteinases from Asp. oryzae and Str. griseus. The inhibitor forms a complex with chymotrypsin at a molar ratio of 1:1, has a molecular weight of about 20,000 and a low content of half-cysteine.

Publication types

  • English Abstract

MeSH terms

  • Chymotrypsin / antagonists & inhibitors*
  • Molecular Weight
  • Protease Inhibitors / isolation & purification*
  • Protease Inhibitors / pharmacology
  • Seeds / analysis*

Substances

  • Protease Inhibitors
  • Chymotrypsin