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%).
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