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Oxidation rates of some desialylated glycoproteins by galactose oxidase
Authors:G Avigad
Affiliation:1. Ministry of Education (MOE) Key Laboratory of Environmental Remediation and Ecosystem Health, College of Environmental and Resources Science, Zhejiang University, Hangzhou, 310058, People’s Republic of China;2. PEIE Research Chair for the Development of Industrial Estates and Free Zones, Center for Environmental Studies and Research, Sultan Qaboos University, Al-Khoud 123, Muscat, Oman;3. Institute of Crop Science and Zhejiang Key Laboratory of Crop Germplasm, Zhejiang University, Hangzhou, 310058, China;1. Department of Chemistry and Chemical Engineering, MOE Engineering Research Center of Forestry Biomass Materials and Bioenergy, Beijing Forestry University, Beijing, 100083, PR China;2. Institution for the Comprehensive Utilization of Wild Plants, Nanjing, 210042, PR China;1. Aix-Marseille Université, Unité de Recherche sur les Maladies Infectieuses et Tropicales Émergentes, UM63, CNRS 7278, IRD 198, INSERM 1095, Marseille, France;2. Special Infectious Agents Unit, King Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia;3. Assistance Publique des Hôpitaux de Marseille, BioSTIC, Pôle de Santé Publique, Marseille, France;4. Aix-Marseille Université, UMR912 SESSTIM (AMU-INSERM-IRD), Marseille, France;1. Jiangxi Key Laboratory of Disaster Prevention-Mitigation and Emergency Management, East China Jiaotong University, Nanchang, China;2. School of Civil and Architecture Engineering, Nanchang Institute of Technology, Nanchang, China;3. Department of Materials Science and Engineering, National University of Singapore, Singapore;1. Shanghai Cancer Center, Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, PR China;2. Department of Chemistry, Fudan University, Shanghai 200433, PR China;3. Key Laboratory of Glycoconjugates Research Ministry of Public Health, Fudan University, Shanghai 200032, PR China;1. Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal;2. Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), 4200-135 Porto, Portugal;3. Instituto de Ciências Biomédicas Abel Salazar (ICBAS), University of Porto, 4050-313 Porto, Portugal;4. Faculty of Medicine of the University of Porto, 4200-319 Porto, Portugal
Abstract:Patterns of oxidation of dilute solutions of desialylated fetuin and submaxillary mucin by galactose oxidase have been examined. A significant portion (20-40%) of the terminal galactosyls exposed on the glycoproteins, which theoretically were expected to be accessible to the enzyme, was not oxidized. In comparison, galactosyls in oligosaccharides released from completely desialylated glycoproteins were oxidized more effectively with an apparently lower degree of crypticity to the enzyme. Partial desialylation usually resulted in a reduction of both the rate and the final level of substrate oxidation. A second cycle of oxidation of a desialylated substrate earlier oxidized by galactose oxidase and then reduced by NaB3H4 revealed a selectivity in the pattern of galactosyl oxidation. The same galactosyl residues oxidized in the first cycle were again the most susceptible to oxidation in the second cycle, leaving unmodified the same fraction of galactosyls throughout both cycles. The relevance of these results to the application of the galactose oxidase-NaBH4 procedure for detecting and measuring desialylated glycoconjugates in solution and in biological membranes is discussed.
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