Purification and Some Properties of a Proteinase Inhibitor (DE-1) fromPeltophorum africanum(Weeping wattle) Seed
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (2) , 1515-1522
- https://doi.org/10.1515/bchm2.1981.362.2.1515
Abstract
A proteinase inhibitor (DE-1) from the seed of P. africanum (weeping wattle) was purified by chromatographic procedures involving Sephadex G-50, DEAE-cellulose and DEAE-Sepharose. It comprises 162 amino acid residues (MW 18,000 Da [daltons]) including 4 half-cystine residues and resembles the Kunitz-type proteinase inhibitors. The N-terminal primary structure of DE-1 showed homology with Kunitz soybean trypsin inhibitor and also with the proteinase inhibitors from Albizzia julibrissin and Erythrina latissima seeds. The inhibitor stoichiometrically inhibited trypsin and also .alpha.-chymotrypsin in the molar ratio of 1:1 and represents a Kunitz-type double-headed proteinase inhibitor.This publication has 17 references indexed in Scilit:
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