Heparan Sulfate Structure: Methods to Study N-Sulfation and NDST Action

Autor:	Lena Kjellén, Beata Filipek-Górniok, Tabea Dierker, Anders Dagälv, Inger Eriksson, Anders Lundequist
Rok vydání:	2014
Předmět:	chemistry.chemical_classification biology Chemistry Perlecan Heparan sulfate Polysaccharide carbohydrates (lipids) chemistry.chemical_compound Enzyme Sulfation Biochemistry Glucosamine biology.protein Sulfate Heparan Sulfate Biosynthesis
Zdroj:	Methods in Molecular Biology ISBN: 9781493917136 Methods in Molecular Biology ISBN: 9781071613979
DOI:	10.1007/978-1-4939-1714-3_17
Popis:	Heparan sulfate proteoglycans are important modulators of cellular processes where the negatively charged polysaccharide chains interact with target proteins. The sulfation pattern of the heparan sulfate chains will determine which proteins will bind and the affinity of the interactions. The N-deacetylase/N-sulfotransferase (NDST) enzymes are of key importance during heparan sulfate biosynthesis when the sulfation pattern is determined. In this chapter, metabolic labeling of heparan sulfate with [35S]sulfate or [3H]glucosamine in cell cultures is described, in addition to characterization of polysaccharide chain length and degree of N-sulfation. Methods to measure NDST enzyme activity are also presented.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0b4e5253bb2abec18b66747f669cbfc https://doi.org/10.1007/978-1-4939-1714-3_17 Zobrazit plný text záznamu