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Biotechnology letters. : a monthly journal for the rapid communication of results and developments in all aspects of biotechnology, v.25 no.4, 2003년, pp.353 - 358
Kim, Wook-Dong (Institute of Applied Biochemistry, University of Tsukuba, Ibaraki 305-8572, Japan) , Kaneko, Satoshi (Molecular Function Laboratory, National Food Research Institute, Kannon-dai 2-1-12, Tsukuba, Ibaraki 305-8642, Japan) , Park, Gwi-Gun (Department of Food Engineering and Biotechnology, Kyungwon University, Kyunggi-do 461-701, Korea) , Tanaka, Hideo (Institute of Applied Biochemistry, University of Tsukuba, Ibaraki 305-8572, Japan) , Kusakabe, Isao (Institute of Applied Biochemistry, University of Tsukuba, Ibaraki 305-8572, Japan) , Kobayashi, Hideyuki (Molecular Function Laboratory, National Food Research Institute, Kannon-dai 2-1-12, Tsukuba, Ibaraki 305-8642, Japan)
From 100 g sunflower seeds, 1.2 mg purified &agr;-galactosidase was obtained with an overall yield of 51%. The &agr;-galactosidase acted on both terminal &agr;-galactosyl residues and side-chain &agr;-galactosyl residues of the galactomanno-oligosaccharides and galactomannans. The cDNA coding for sunflower &agr;-galactosidase was cloned and the deduced amino acid sequence revealed that the mature enzyme consisted of 363 amino acid residues with a molecular weight of 40 263. Seven cysteine residues were found but no putative N-glycosylation sites were present in the sequence. The deduced amino acid sequences of mature enzyme and &agr;-galactosidases from coffee, guar and Mortierella vinacea &agr;-galactosidase II showed over 81%, 77%, and 47% homology, respectively. These enzymes are classified into the third group in which the enzyme has no insertion sequence and a broad specificity on galactomanno-oligosaccharides compared to the other groups.
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