Abstract
A 7514-Da chymotrypsin inhibitor was isolated from the seed extract of Momordica cochinchinensis (Family Cucurbitaceae) by chromatography on chymotrypsin-Sepharose 4B and subsequently by C18 reversed-phase HPLC. This inhibitor, named MCoCl, possessed remarkable thermostability and was stable from pH 2 to 12. MCoCl also inhibited subtilisin, but had at least 50-fold lower inhibitory activity towards trypsin and elastase. Amino acid sequencing of a peptide fragment of MCoCl revealed a sequence of 23 amino acids. Comparison of this sequence and the molecular mass with those of other protease inhibitors suggests that MCoCl belongs to the potato I inhibitor family.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Chromatography, Affinity
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Chromatography, High Pressure Liquid / methods
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Chymotrypsin / antagonists & inhibitors*
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Molecular Sequence Data
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Molecular Weight
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Momordica / enzymology*
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Pancreatic Elastase / antagonists & inhibitors
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Peptide Fragments / genetics
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Seeds / enzymology*
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Sequence Alignment
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Serine Proteinase Inhibitors / chemistry*
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Serine Proteinase Inhibitors / genetics
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Serine Proteinase Inhibitors / isolation & purification
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Serine Proteinase Inhibitors / pharmacology*
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Solanum tuberosum / enzymology
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Subtilisins / antagonists & inhibitors
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Trypsin / metabolism
Substances
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Peptide Fragments
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Serine Proteinase Inhibitors
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Subtilisins
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Chymotrypsin
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Pancreatic Elastase
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Trypsin