Interaction between Acidic Polysaccharides and Proteins(Biochemistry & Molecular Biology)
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概要
- 論文の詳細を見る
There was an ionic interaction between acidic polysaccharides (APS) and proteins at the pH range in which APS were negatively charged and proteins were positively charged, and in enzymes the interaction was detected as a change in the enzyme activity. At pH 4.7, acid phosphatase (pI, 5.4), α-glucosidase (pI, 5.7), and β-glucosidase (pI, 7.3) were inhibited by APS to various extents. On the other hand, α-glucosidase and alkaline phosphatase (pI, 4.5) were not inhibited by APS at pH 6.8 and 9.8, respectively, most of these two enzymes being negatively charged at the respective pHs. Sulfated polysaccharides combined with hemoglobin (pI, 6.8 〜 7.0) by an ionic bond at pH 2 to make hemoglobin unsusceptible to proteolysis by pepsin, but polyuronides which were not charged at this pH did not affect hydrolysis of hemoglobin.
- 社団法人日本農芸化学会の論文
- 2003-08-23
著者
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Minami Yuji
Department Of Biochemical Science And Technology Faculty Of Agriculture Kagoshima University
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Tadera Kenjiro
Department Of Biochemical Science And Technology Faculty Of Agriculture Kagoshima University
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CHOHCHI Miki
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University
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Tadera Kenjiro
Department of Biochemical Science and Technology
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TADERA Kenjiro
Department of Agricultural Chemistry, Faculty of Agriculture, Kagoshima University
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