Glycation of native hyaluronidase and its chondroitin sulfate modified form was studied with N-acethylglucosamine, N-acethylgalactosamine and their mixture, as well as hyaluronan fragments (n = 0-4) and their mixture. The modified form of hyaluronidase exhibited higher inactivation than native enzyme. The chondroitin sulfate modification of hyaluronidase altered its surface electrostatic potential, but this effect was not crucial for inactivation of hyaluronidase derivatives. The observed picture of the glycation action on hyaluronidase derivatives was opposite for glycation with mono- and di-saccharides. Such results give us the informative enzyme test for in vivo system in order to determine the dominant type of glycation agents in bloodstream and its origin.
Turashev A.D., Tischenko E.G., Maksimenko A.V. (2011) Electrostatic interactions determine glycation of hyaluronidase derivatives with n-acethylhexosamines?. Biomeditsinskaya Khimiya, 57(6), 624-634.
Turashev A.D. et al. Electrostatic interactions determine glycation of hyaluronidase derivatives with n-acethylhexosamines? // Biomeditsinskaya Khimiya. - 2011. - V. 57. -N 6. - P. 624-634.
Turashev A.D. et al., "Electrostatic interactions determine glycation of hyaluronidase derivatives with n-acethylhexosamines?." Biomeditsinskaya Khimiya 57.6 (2011): 624-634.
Turashev, A. D., Tischenko, E. G., Maksimenko, A. V. (2011). Electrostatic interactions determine glycation of hyaluronidase derivatives with n-acethylhexosamines?. Biomeditsinskaya Khimiya, 57(6), 624-634.
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