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Updated: Sep 20, 2026

Activation and Conjugation of Soluble Polysaccharides using 1-Cyano-4-Dimethylaminopyridine Tetrafluoroborate (CDAP)
Published on: June 14, 2021
Interaction between acidic polysaccharides and proteins
Kenjiro Tadera1, Yuji Minami, Miki Chohchi
1Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Korimoto 1-21-24, Kagoshima 890-0065, Japan. tadera@chem.agri.kagoshima-u.ac.jp
Abstract:
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), alpha-glucosidase (pI, 5.7), and beta-glucosidase (pI, 7.3) were inhibited by APS to various extents. On the other hand, alpha-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 to approximately 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.
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