Characterisation of a modified protease inhibitor from dormant Echinocloa seeds

S. L. Udupa

Research output: Contribution to journalArticle

Abstract

Inhibitor from E. frumentacea seeds was modified on storage as well as by the addition of mercaptoethanol. The trypsin/chymotrypsin inhibitor, totally devoid of antichymotryptic activity, was purified 500 folds with 17% recovery of the antitryptic activity. It was more stable to heat, cooking, changes in pH, and digestion by proteolytic enzymes than the native inhibitor. It formed a complex with trypsin in 1:1 stoichiometric ratio. Both arginyl and lysyl groups were found to be necessary for its action.

Original languageEnglish
Pages (from-to)307-312
Number of pages6
JournalFitoterapia
Volume69
Issue number4
Publication statusPublished - 01-01-1998
Externally publishedYes

Fingerprint

Trypsin Inhibitors
Mercaptoethanol
Cooking
Enzyme Inhibitors
Protease Inhibitors
Trypsin
Digestion
Seeds
Peptide Hydrolases
Hot Temperature

All Science Journal Classification (ASJC) codes

  • Pharmacology

Cite this

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Characterisation of a modified protease inhibitor from dormant Echinocloa seeds. / Udupa, S. L.

In: Fitoterapia, Vol. 69, No. 4, 01.01.1998, p. 307-312.

Research output: Contribution to journalArticle

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