Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/7444
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Type: Journal article
Title: Highly sensitive sequencing of the sulfated domains of heparan sulfate
Author: Merry, C.
Lyon, M.
Deakin, J.
Hopwood, J.
Gallagher, J.
Citation: Journal of Biological Chemistry, 1999; 274(26):18455-18462
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date: 1999
ISSN: 0021-9258
1083-351X
Statement of
Responsibility: 
Catherine L. R. Merry, Malcolm Lyon, Jon A. Deakin, John J. Hopwood and John T. Gallagher
Abstract: The heparan sulfates (HS) are hypervariable linear polysaccharides that act as membrane co-receptors for growth factors, chemokines, and extracellular matrix proteins. In most instances, the molecular basis of protein recognition by HS is poorly understood. We have sequenced 75% of the sulfated domains (S-domains) of fibroblast HS, including all of the major ones. This analysis revealed tight coupling of N- and 2-O-sulfation and a low frequency but precise positioning of 6-O-sulfates, which are required functional groups for HS-mediated activation of the fibroblast growth factors. S-domain sequencing was conducted using a novel and highly sensitive method based on a new way of reading the sequence from high performance liquid chromatography separation profiles of metabolically labeled HS-saccharides following specific chemical and enzymatic scission. The implications of the patterns seen in the sulfated domains for better understanding of the synthesis and function of HS are discussed.
Keywords: 3T3 Cells
Animals
Mice
Sulfates
Heparitin Sulfate
Chromatography, Gel
Chromatography, High Pressure Liquid
Carbohydrate Sequence
Molecular Sequence Data
DOI: 10.1074/jbc.274.26.18455
Appears in Collections:Aurora harvest
Paediatrics publications

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