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:
- Studies on Soybean Trypsin InhibitorsThe Journal of Biochemistry, 1977
- The partial amino acid sequence of trypsin inhibitor II from garden bean, Phaseolus vulgaris, with location of the trypsin and elastase-reactive sitesJournal of Biological Chemistry, 1975
- The Amino Acid Sequences of Three Toxins (CM-10, CM-12 and CM-14) fromNaja haje annulifera(Egyptian Cobra) VenomHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1975
- Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gelsBiochemical and Biophysical Research Communications, 1967
- Halogenation of tyrosine during acid hydrolysisBiochimica et Biophysica Acta, 1963
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959
- A spectrophotometric determination of trypsin and chymotrypsinBiochimica et Biophysica Acta, 1955
- Naturally Occurring Trypsin InhibitorsAdvances in protein chemistry, 1954
- Differentiation of Soy Bean Antitryptic FactorsExperimental Biology and Medicine, 1946