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Effects of divalent cations on bovine testicular hyaluronidase catalyzed transglycosylation of chondroitin sulfates
- Kakizaki, Ikuko, Nukatsuka, Isoshi, Takagaki, Keiichi, Majima, Mitsuo, Iwafune, Mito, Suto, Shinichiro, Endo, Masahiko
- Biochemical and biophysical research communications 2011 v.406 no.2 pp. 239-244
- barium, cations, cattle, chondroitin sulfate, copper, hyaluronic acid, hyaluronoglucosaminidase, manganese, sulfates, zinc
- Glycosaminoglycans were prepared as salts of different divalent cations and tested as donors in bovine testicular hyaluronidase catalyzed transglycosylation reactions. All of the metal cations examined had similar binding efficiency of divalent cations to hyaluronan. However, cations bound with different efficiencies to chondroitin sulfate species and the differences were marked in the case of chondroitin 6-sulfate; the numbers of cations bound per disaccharide unit were estimated to be 0.075 for Mn, 1.231 for Ba, 0.144 for Zn, and 0.395 for Cu. While barium salt of chondroitin sulfates enhanced transglycosylation, the zinc salt of chondroitin sulfates inhibited transglycosylation. Therefore, by selecting the proper divalent cation salt of chondroitin sulfates as a donor in the transglycosylation reaction it is possible to improve the yields of the products.