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Identification of side-reaction products generated during the ammonia-catalyzed release of N-glycans.
Liew, Chia Yen; Chen, Jien-Lian; Tsai, Shang-Ting; Ni, Chi-Kung.
Afiliación
  • Liew CY; Institute of Atomic and Molecular Sciences, Academia Sinica, Taipei, 10617, Taiwan; International Graduate Program of Molecular Science and Technology, National Taiwan University, Taipei, 10617, Taiwan; Molecular Science and Technology, Taiwan International Graduate Program, Academia Sinica, Taipei,
  • Chen JL; Institute of Atomic and Molecular Sciences, Academia Sinica, Taipei, 10617, Taiwan.
  • Tsai ST; Institute of Atomic and Molecular Sciences, Academia Sinica, Taipei, 10617, Taiwan; Department of Applied Chemistry, National Chiayi University, Chiayi City, 600355, Taiwan.
  • Ni CK; Institute of Atomic and Molecular Sciences, Academia Sinica, Taipei, 10617, Taiwan; Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan. Electronic address: ckni@po.iams.sinica.edu.tw.
Carbohydr Res ; 522: 108686, 2022 Dec.
Article en En | MEDLINE | ID: mdl-36202042
N-linked glycosylation is one of the most important post translational modification of proteins. Various analytical techniques are used for the structural identification of the N-glycans released from proteins through various enzymatic and chemical methods. Although very few side-reaction products are generated during the enzymatic release of N-glycans, this method is expensive and suitable only for small quantities of samples. By contrast, chemical methods can be used for large quantities of samples; however, various side-reaction products are generated when chemical methods are used. Recently, the ammonia-catalyzed release of N-glycans from proteins has been reported to be associated with no typical side reactions. In the present study, we discovered a new side reaction: the epimerization of N-acetylglucosamine present at the reducing end of N-glycans to N-acetylmannosamine. The product of this side reaction interfered with the structural identification N-glycans. We propose a simple method that can help identify this artifact N-glycan isomer and eliminate the aforementioned interference. This simple method widens the applicability of ammonia-catalyzed reactions for N-glycan release from proteins, and is also suitable for N-glycans released using any other alkaline solutions.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glicoproteínas / Amoníaco Tipo de estudio: Diagnostic_studies Idioma: En Revista: Carbohydr Res Año: 2022 Tipo del documento: Article Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glicoproteínas / Amoníaco Tipo de estudio: Diagnostic_studies Idioma: En Revista: Carbohydr Res Año: 2022 Tipo del documento: Article Pais de publicación: Países Bajos