PMID: 1266Dec 1, 1975

The trypsin and chymotrypsin inhibitors in chick peas (Cicer arietinum L.). Purification and properties of the inhibitors

European Journal of Biochemistry
M BelewL Sundberg

Abstract

From a crude extract of chick peas (Cicer arietinum L.) inhibitors of trypsin and chymotrypsin were isolated by affinity chromatography on a column of trypsin-Sepharose 6B. The content of inhibitors was found to be 1.5 g/kg. They were further separated into six isoinhibitors by ion-exchange chromatography on DEAE-Sephadex A-25. Two of the isoinhibitors accounted for about 50% of the isolated inhibitors and were further purified to a homogeneous state. The isoinhibitors had a molecular weight of about 10000 as determined by molecular-sieve chromatography on Sephadex G-75. They were stable towards extremes of pH and temperatures up to 75 degrees C or towards digestion by pepsin. They were also stable in 6 M urea but not in 6 M guanidine-HCl. The intact inhibitors were destroyed when the peas were cooked at 100 degrees C or when they were toasted at 130 degrees C. The four major inhibitors had similar amino acid compositions and did not contain detectable amounts of free sulfhydryl groups, tryptophan or carbohydrate. Cysteine is the dominant amino acid residue in all of them and accounted for about 20% of their amino acid content. The isoelectric point of the isoinhibitors lies in the range of pH 4.9-8.6 and two of the major inhib...Continue Reading

References

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Citations

Jan 1, 1987·Plant Foods for Human Nutrition·Y P Gupta
Feb 26, 2013·Insect Molecular Biology·Y R ChikateAshok P Giri
Mar 10, 2017·Preparative Biochemistry & Biotechnology·Tooba Naz ShamsiSadaf Fatima
Jan 1, 1984·Die Nahrung·G MossorB Romanowska
Aug 11, 2001·Journal of Enzyme Inhibition·J VioqueF Millán

Related Concepts

Chromatography, Affinity
Avazyme
Drug Stability
Guanidines
Hydrogen-Ion Concentration
Pepsin 3
Plant Proteins
Trypsin Inhibitors
Carmol

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