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SCIE SCOPUS
Amino Acid Sequence of a Probable Amylase / Protease Inhibitor from Rice Seeds
유연규 , 정진하 , 서세원 ( Audree Fowler )
UCI I410-ECN-0102-2009-470-007037289
This article is 4 pages or less.

The primary structure of a 9-kDalton basic protein from rice seeds was determined by gas-phase sequencing of the intact protein and peptides derived from it by digestion with trypsin, chymotrypsin, and endopeptidase Lys-K. The protein consists of a single polypeptide chain of 91 amino acid residues with a calculated molecular mass of 8909 Da. It is rich in alanine, serine, glycine, and cysteine. The eight cysteines form four disulfide bonds. There is no methionine, histidine, phenylalanine, or tryptophan. The sequence is highly homologous with an α-amylase inhibitor, I-2, from seeds of Indian finger millet and a 10-kDa barley seed protein, also called a probable amylase/protease inhibitor. In analogy with the barley protein, the purified protein is tentatively called a rice probable amylase/protease inhibitor (PAPI). The rice PAPI does not show inhibitory activities against proteases and amylases tested. However, it shows a thioredoxin-like activity comparable to those of purothionins and hordothionins.

[자료제공 : 네이버학술정보]
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