Abstract
A proteinaceous alpha-amylase inhibitor (CLAI) was purified from Cicer arietinum seeds. It had a molecular mass of 25.947 kDa and inhibited alpha-amylases from plants and mammals. Analysis of the amino acid sequence of a polypeptide from CLAI showed that it was different from other known alpha-amylase inhibitors, but had high identity to legumins from Cicer arietinum (100%) and Vicia faba var. minor (90%).
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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Animals
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Chromatography, Liquid
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Cicer / chemistry*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / isolation & purification
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Enzyme Inhibitors / pharmacology*
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Humans
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Legumins
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Molecular Sequence Data
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Plant Proteins / chemistry
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Plant Proteins / isolation & purification
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Plant Proteins / pharmacology*
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Seeds / chemistry*
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alpha-Amylases / antagonists & inhibitors*
Substances
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Enzyme Inhibitors
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Plant Proteins
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alpha-Amylases