Preparation of hyaluronan O-methylester and its enzymatic degradation
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Authors
Hirano, K.
Sakai, Shinobu
Ishikawa, T.
Avci, F.Y.
Linhardt, Robert J.
Toida, T.
Issue Date
2005
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
Abstract
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 4.2.2.5) from Flavobacterium heparinum and chondroitin ACII lyase (EC 4.2.2.5) 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.
Description
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.
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.
Full Citation
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.
Publisher
Elsevier