Characterization of a novel legumin alpha-amylase inhibitor from chickpea (Cicer arietinum L.) seeds.
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%).
Hao
Xiaoyan
X
State Key Laboratory of Crop Genetics and Germplasm Enhancement, National Center for Soybean Improvement, Nanjing Agricultural University, Nanjing, China.
Li
Jiangui
J
Shi
Qinghua
Q
Zhang
Jusong
J
He
Xiaoling
X
Ma
Hao
H
D000595:Amino Acid Sequence; D000818:Animals; D002853:Chromatography, Liquid; D029863:Cicer / Q000737:chemistry*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D006801:Humans; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D012639:Seeds / Q000737:chemistry*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*; D000097793:Legumins
D004791:Enzyme Inhibitors; D010940:Plant Proteins; D000516:alpha-Amylases; D000097793:Legumins