Purification and Some Properties of Two Proteinase Inhibitors From Erythrina acanthocarpa Seed
- 1 July 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Natural Products
- Vol. 45 (4) , 427-433
- https://doi.org/10.1021/np50022a011
Abstract
Two proteinase inhibitors (DE-1 and DE-2) were purified from E. acanthocarpa seed by gel filtration followed by ion exchange chromatography on DEAE-cellulose and DEAE-sepharose. They contain 163-164 amino acids (MW 18,000) including 4 half-cystine residues and resemble the Kunitz-type proteinase inhibitors. The N-terminal amino acid sequence of DE-1 also shows homology with those of the Kunitz-type inhibitors. For DE-2, no free N-terminal amino acid was found. DE-1 contains a potent inhibitor for porcine trypsin and bovine .alpha.-chymotrypsin. Inhibitor DE-2 inhibits .alpha.-chymotrypsin strongly and it has practically no action on trypsin.This publication has 4 references indexed in Scilit:
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