Purification and Some Properties of Two Proteinase Inhibitors (DE-1 and DE-3) fromErythrina latissima(Broad-Leaved Erythrina) Seed
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (1) , 531-538
- https://doi.org/10.1515/bchm2.1981.362.1.531
Abstract
DE-1 inhibits bovine chymotrypsin and not bovine trypsin, DE-3 inhibits trypsin but not chymotrypsin. The MW and the amino acid compositions of the 2 inhibitors resemble the corresponding properties of the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-3 showed homology with soybean trypsin inhibitor (Kunitz) and also with the proteinase inhibitors (A-II and B-II) from Albizzia julibrissin seed.This publication has 20 references indexed in Scilit:
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