Novel products in hyaluronan digested by bovine testicular hyaluronidase |
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Authors: | Fengchao Chen Ikuko Kakizaki Masanori Yamaguchi Kaoru Kojima Keiichi Takagaki Masahiko Endo |
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Affiliation: | (1) Department of Glycotechnology, Center for Advanced Medical Research, Hirosaki University Graduate School of Medicine, 5 Zaifu-cho, Hirosaki 036-8562, Japan |
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Abstract: | When the products of hyaluronan (HA) digested by bovine testicular hyaluronidase (BTH) were analyzed by high-performance liquid
chromatography (HPLC), minor peaks were detected just before the main even-numbered oligosaccharide peaks. The amount of each
minor peak was dependent on the reaction conditions for transglycosylation, rather than hydrolysis, by the BTH. Mainly based
on HPLC and MS analysis, each minor peak was found to correspond to its oligosaccharide with one N-acetyl group removed from the reducing terminal N-acetylglucosamine. Enzymatic studies showed that the N-deacetylation activity was closely related to reaction temperature, pH, and the concentration of NaCl contained in the buffer,
and glycosaminoglycan types and chain lengths of substrates. These findings strongly suggest that the N-deacetylation reaction in minor peaks was due to a novel enzyme contaminant in the BTH, N-deacetylase, that carries out N-deacetylation at the reducing terminal N-acetylglucosamine of oligosaccharides and is dependent on HA hydrolysis by BTH. |
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Keywords: | Bovine testicular hyaluronidase Hyaluronan oligosaccharide N-Deacetylase N-Deacetylated oligosaccharide N-Deacetylation |
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