Iaroslav Kosov
Research Subjects
Research Interests
Iaroslav Kosov has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Christopher J. Gray
University of Manchester
2 shared publications - Edward Pallister
Analytical Sciences, BioPharmaceuticals Development, R&D, AstraZeneca, Cambridge CB21 6GH, U.K.
2 shared publications - Josef Voglmeir
Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, 1 Weigang, 210095 Nanjing, China
2 shared publications - Kun Huang
Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, UK
2 shared publications - Louis P. Conway2 shared publications
- Michel Riese2 shared publications
Latest Publications
- Open Access
- 31 August 2017
- Published by American Chemical Society (ACS) in ChemRxiv
Development and application of a highly α2,6-selective pseudosialidase
In this manuscript we address an important gap in our current carbohydrate active enzyme toolbox, by developing a highly a2,6-selective (over a2,3-selective) de facto sialidase that is necessary both for glycan analysis and glycoconjugate remodeling. Both glycosidic linkages are commonly found in animal biology and each has been shown to have distinct biological function. Our approach is novel in that it harnesses the high selectivity of known glycosyltransferases ‘in reverse’ for effective hydrolysis, converting transferases to hydrolases by reaction engineering. More specifically, we demonstrate that the a2,6-specific pseudosialidase activity of Photobacterium sp. JT-ISH-224 a2,6-sialyltransferase can be used effectively for highly a2,6 selective hydrolysis on a broad range of analytes: small synthetic probes, isolated complex glycans and complex mixtures of glycoproteins.
- 31 August 2017
- Published by American Chemical Society (ACS) in ChemRxiv
Open AccessDevelopment and application of a highly α2,6-selective pseudosialidase
In this manuscript we address an important gap in our current carbohydrate active enzyme toolbox, by developing a highly a2,6-selective (over a2,3-selective) de facto sialidase that is necessary both for glycan analysis and glycoconjugate remodeling. Both glycosidic linkages are commonly found in animal biology and each has been shown to have distinct biological function. Our approach is novel in that it harnesses the high selectivity of known glycosyltransferases ‘in reverse’ for effective hydrolysis, converting transferases to hydrolases by reaction engineering. More specifically, we demonstrate that the a2,6-specific pseudosialidase activity of Photobacterium sp. JT-ISH-224 a2,6-sialyltransferase can be used effectively for highly a2,6 selective hydrolysis on a broad range of analytes: small synthetic probes, isolated complex glycans and complex mixtures of glycoproteins.
- Open Access
- 1 January 2017
- Published by American Chemical Society (ACS) in ChemRxiv
Development and application of a highly α2,6-selective pseudosialidase
In this manuscript we address an important gap in our current carbohydrate active enzyme toolbox, by developing a highly a2,6-selective (over a2,3-selective) de facto sialidase that is necessary both for glycan analysis and glycoconjugate remodeling. Both glycosidic linkages are commonly found in animal biology and each has been shown to have distinct biological function. Our approach is novel in that it harnesses the high selectivity of known glycosyltransferases ‘in reverse’ for effective hydrolysis, converting transferases to hydrolases by reaction engineering. More specifically, we demonstrate that the a2,6-specific pseudosialidase activity of Photobacterium sp. JT-ISH-224 a2,6-sialyltransferase can be used effectively for highly a2,6 selective hydrolysis on a broad range of analytes: small synthetic probes, isolated complex glycans and complex mixtures of glycoproteins.
- 1 January 2017
- Published by American Chemical Society (ACS) in ChemRxiv
Open AccessDevelopment and application of a highly α2,6-selective pseudosialidase
In this manuscript we address an important gap in our current carbohydrate active enzyme toolbox, by developing a highly a2,6-selective (over a2,3-selective) de facto sialidase that is necessary both for glycan analysis and glycoconjugate remodeling. Both glycosidic linkages are commonly found in animal biology and each has been shown to have distinct biological function. Our approach is novel in that it harnesses the high selectivity of known glycosyltransferases ‘in reverse’ for effective hydrolysis, converting transferases to hydrolases by reaction engineering. More specifically, we demonstrate that the a2,6-specific pseudosialidase activity of Photobacterium sp. JT-ISH-224 a2,6-sialyltransferase can be used effectively for highly a2,6 selective hydrolysis on a broad range of analytes: small synthetic probes, isolated complex glycans and complex mixtures of glycoproteins.