Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 406236
Title Characterization of PmHS2 glycosyltransferases for the controlled synthesis of heparosan : a precursor of heparin and heparan sulfate
Author(s) Chavaroche, A.A.E.
Source University. Promotor(en): Gerrit Eggink. - S.l. : s.n. - ISBN 9789085858805 - 169
Department(s) Bioprocess Engineering
VLAG
Publication type Dissertation, internally prepared
Publication year 2011
Keyword(s) industriële microbiologie - heparine - synthese - recombinant eiwitten - industrial microbiology - heparin - synthesis - recombinant proteins
Categories Industrial Microbiology
Abstract

Heparin (Hep), a highly sulfated and complex glycosaminoglycan polysaccharides, is worldwide used as an anticoagulant compound to prevent blood clotting during surgery. Heparin and its analogue, heparan sulfate (HS), have a large potential for medical applications. Nevertheless, the utilization of Hep/HS-based drugs in new therapeutic settings requires the synthesis of well-defined heparin and heparan sulfate-like molecules. Since neither the extraction from animal derivatives, nor the chemical synthesis, are suitable for the production of a large variety of defined Hep/HS polymers, there is a general interest in developing alternative systems enabling to tightly control Hep/HS synthesis. During the synthesis of heparin and heparan sulfate, the polymerization of the polysaccharide backbone, known as heparosan, determines the chain length and the size distribution of these polymers. Here, the Pasteurella multocida heparosan synthase PmHS2, a bacterial enzyme catalyzing the formation of heparosan polymers, was studied in detail in order to develop methods to control the polymer elongation.

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