期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 67, 期 8, 页码 1832-1835出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.67.1832
关键词
dehydrin; group2 LEA protein; soybean seed protein; cryoprotective activity
To characterize the molecular weight diversity of seed dehydrin among soybean cultivars, 26/27-kDa soybean dehydrins were purified and compared in peptide mapping patterns, partial amino acid sequences, and cryoprotective activity on enzyme. In reverse phase chromatograms of their trypsin digests, we detected several distinctive peaks, one of which was attributed to a part of the internal glycine-rich region. Partial amino acid sequences of peptide fragments from trypsin and S. aureus V8 protease cleavage were found to be identical to the Mat9 translation. The CP50 of purified 26/27-kDa dehydrins were estimated to be 0.30 and 0.11 mum, respectively.
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