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Type: Journal article
Title: Analysis of normal and mutant iduronate-2-sulphatase conformation
Author: Parkinson-Lawrence, E.
Turner, C.
Hopwood, J.
Brooks, D.
Citation: Biochemical Journal, 2005; 386(2):395-400
Publisher: Portland Press
Issue Date: 2005
ISSN: 0264-6021
Abstract: Mammalian sulphatases (EC 3.1.6) are a family of enzymes that have a high degree of similarity in amino acid sequence, structure and catalytic mechanism. IDS (iduronate-2-sulphatase; EC is a lysosomal exo-sulphatase that belongs to this protein family and is involved in the degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate. An IDS deficiency causes the lysosomal storage disorder MPS II (mucopolysaccharidosis type II). To examine the structural alterations in heat-denatured and mutant IDS, a panel of four monoclonal antibodies was raised to the denatured protein and used as probes of protein conformation. The linear sequence epitope reactivity of a polyclonal antibody raised against the native protein and the monoclonal antibodies were defined and mapped to distinct regions on the IDS protein. The antigenicity of native IDS was higher in regions without glycosylation, but reactivity was not restricted to protein surface epitopes. One monoclonal epitope was relatively surface accessible and in close proximity to an N-linked glycosylation site, while three others required additional thermal energy to expose the epitopes. The monoclonal antibodies demonstrated the capacity to differentiate progressive structural changes in IDS and could be used to characterize the severity of MPS type II in patients based on variable denatured microstates.
Keywords: Liver
Central Nervous System
Cell Line
CHO Cells
Endothelial Cells
Mucopolysaccharidosis II
Iduronate Sulfatase
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Antibodies, Monoclonal
Amino Acid Substitution
Epitope Mapping
Age of Onset
Protein Conformation
Protein Denaturation
Models, Molecular
Child, Preschool
Hot Temperature
Rights: The Biochemical Society, London ©2005
DOI: 10.1042/BJ20040739
Appears in Collections:Aurora harvest 2
Paediatrics publications

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