Sequencing complex polysaccharides

Glycosaminoglycans are complex polysaccharides that exist at the cell/extracellular matrix interface. As such, these information-dense molecules are key regulators of extracellular signals. However, to date, there has been a lack of effective biochemical and analytical tools for the analysis of glycosaminoglycan structure and hence, there is very little understanding of exactly how glycosaminoglycan structure impinges on function. Development of such tools is especially important for a key subset of glycosaminoglycans, i.e., heparin/heparan sulfate-like glycosaminoglycans (HLGAGs). As a first step in the development of tools to study HLGAG structure, biochemical studies were completed on the heparinases, a family of three HLGAG-degrading enzymes from Flavobacterium heparinum. With heparinase I, it was found that calcium is a necessary cofactor for optimal activity and that two putative calcium coordinating motifs exist in heparinase I. With heparinase II, a single cysteine and three histidines were found to be critical for proper enzymatic function. Finally, with heparinase III, two histidines were found to be catalytically important.

Department dc:contributor.department

Massachusetts Institute of Technology. Division of Bioengineering and Environmental Health

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2001

Author dc:creator

• Shriver, Zachary (Zachary Holmes), 1973-

Advisor dc:contributor.advisor

• Ram Sasisekharan.

• Division of Bioengineering and Environmental Health.

Statement dc:rights

• MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/17515

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/17515