PMID: 10963446Aug 30, 2000Paper

Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties

Phytochemistry
Maria Lígia R MacedoJosé C Novello

Abstract

A trypsin inhibitor from Dimorphandra mollis seeds was isolated to apparent homogeneity by a combination of ammonium sulfate precipitation, gel filtration, ion-exchange and affinity chromatographic techniques. SDS-PAGE analysis gave an apparent molecular weight of 20 kDa, and isoelectric focusing analysis demonstrated the presence of three isoforms. The partial N-terminal amino acid sequence of the purified protein showed a high degree of homology with various members of the Kunitz family of inhibitors. This inhibitor, which inhibited trypsin activity with a Ki of 5.3 x 10(-10) M, is formed by a single polypeptide chain with an arginine residue in the reactive site.

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Citations

May 6, 2011·Applied Biochemistry and Biotechnology·Jing-Jun RuanJi-Rong Shao
Sep 5, 2002·Biochemical and Biophysical Research Communications·A Soares-CostaF Henrique-Silva
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Feb 24, 2009·Biochemistry. Biokhimii︠a︡·Zhuang KangLin-fang Du
Aug 30, 2008·Biological Chemistry·Maria Luiza Vilela Oliva, Uemura Misako Sampaio
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Apr 2, 2011·Peptides·Jing-Jun RuanXue-Yi Han
Dec 24, 2008·Toxicon : Official Journal of the International Society on Toxinology·Gláucia C MelloEdson Antunes
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Mar 28, 2007·International Immunopharmacology·María F TroncosoCarlota Wolfenstein-Todel
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Apr 7, 2010·Biochimie·Maria Luiza V OlivaMisako U Sampaio
Feb 24, 2015·Applied Biochemistry and Biotechnology·Muni Kumar DokkaSiva Prasad Davuluri
Mar 11, 2009·Anais Da Academia Brasileira De Ciências·Alexandre KanashiroYara M Lucisano-Valim
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Mar 25, 2008·Biochimica Et Biophysica Acta·M H Lingaraju, Lalitha R Gowda

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