Author
Gu, Kenan; Liu, Jian; Pervin, Azra; Linhardt, Robert J.
Other Contributors
Date Issued
1993-06-21
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Comparison of the Activity of Two Chondroitin AC Lyases on Dermatan Sulfate, K. Gu, J. Liu, A. Pervin, R.J. Linhardt, Carbohydrate Research, 244, 369-377 (1993).
Abstract
Chondroitin sulfates are widely distributed in human and animal tissues and are the main constituents of cartilage’. The two major isomeric chondroitin sulfates, A (ChS-A) and C (ChS-C) are isolated as glycosaminoglycan from the proteoglycans present in tissues’. Structural investigations have shown that ChS-A and ChS-C both are co-polymers of D-glucuronic acid and sulfated 2-acetamido-2-deoxy-pgalactose. ChS-A primarily contains 4-sulfated 2-acetamido-2-deoxy-D-galactose residues, while ChS-C primarily contains 6-sulfated 2-acetamido-2-deoxy-o-galactose residues. Dermatan sulfate (DS) is a related glycosaminoglycan, often called chondroitin sulfate B (ChS-B), composed of 4-sulfated 2-acetamido-2-deoxy-ogalactose residues. DS differs from ChS-A and ChS-C since its primary uranic acid residue is L-iduronic acid instead of p-glucuronic acid. Despite these structural differences ChS-A, ChS-C, and DS also contain the minor uranic acid C-S epimer (L-iduronic acid in ChS-A and ChS-C and p-glucuronic acid in DS) in their structures.;
Description
Carbohydrate Research, 244, 369-377; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Carbohydrate Research; https://harc.rpi.edu/;
Access
https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/0008-6215(83)85014-9;
