PMID: 8948493Nov 14, 1996Paper

Primary structure and specificity of a serine proteinase inhibitor from paprika (Capsicum annuum) seeds

Biochimica Et Biophysica Acta
N AntchevaS Pongor

Abstract

Several fractions demonstrating trypsin inhibitory activity were isolated from the seeds of the paprika plant (Capsicum annuum). One of the inhibitors, PSI-1.1, was purified to homogeneity and characterised. The mature form of PSI-1.1 has a molecular mass of 6053 Da and consists of 55 amino acids in a sequence showing over 80% identity with members of the inhibitors of potato-2 family. PSI-1.1 is a potent inhibitor of trypsin (Ki = 4.8 x 10(-10) M) and a somewhat weaker inhibitor of chymotrypsin (Ki = 4.7 x 10(-8) M) and pronase E (Ki = 5.9 x 10(-8) M). PSI-1.1 is resistant to heat up to 85 degrees C, to acidic conditions (down to pH 2.0) and to pepsin digestion, presumably due to its four disulfide bridges.

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Citations

Nov 26, 2002·Trends in Genetics : TIG·Endre BartaSándor Pongor
Oct 15, 1998·Proceedings of the National Academy of Sciences of the United States of America·D De CesareP Sassone-Corsi
Nov 11, 2005·The FEBS Journal·John T Christeller
Oct 27, 2004·Phytochemistry·Alexander V KonarevPeter R Shewry
Apr 10, 2003·The Journal of Biological Chemistry·Isabelle H Barrette-NgMichael N G James
Jun 6, 2003·The Journal of Biological Chemistry·Isabelle H Barrette-NgMichael N G James
Feb 12, 2017·Biotechnology Letters·Shazia RehmanTariq Mahmood
Oct 7, 2004·Archives of Biochemistry and Biophysics·Soghra Khatun HaqRizwan Hasan Khan

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