Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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Preparation of hyaluronan O-methylester and its enzymatic degradation, K. Hirano , S. Sakai, T. Ishikawa, F.Y. Avci, R. J. Linhardt, T. Toida, Carbohydrate Research, 340, 2297-2304, 2005.
A methyl ester of hyaluronan in which the carboxyl groups were fully esterified was prepared using trimethylsilyl diazomethane. This derivative, while not depolymerized by hyaluronan lyases or hyaluronan hydrolases, was a substrate for both chondroitin ACI lyase (EC 188.8.131.52) from Flavobacterium heparinum and chondroitin ACII lyase (EC 184.108.40.206) from Arthrobacter aurescens. The major product isolated in these depolymerization reactions was methyl α-l-threo-hex-4-enepyranosyluronate-(1→3)-2-acetamido-2-deoxy-α,β-d-glucopyranoside as determined by 1H NMR spectroscopy and MALDITOF mass spectrometry.;
Carbohydrate Research, 340, 2297-2304; 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.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;