AI Article Synopsis
- - A methyl ester of hyaluronan was created by fully esterifying its carboxyl groups using a chemical method involving trimethylsilyl diazomethane.
- - This new ester form of hyaluronan was resistant to breakdown by specific enzymes (hyaluronan lyases and hydrolases), but could be degraded by chondroitin lyases from certain bacteria.
- - The main product from the enzyme breakdown was identified as a specific compound through advanced techniques like 1H NMR spectroscopy and MALDI-TOF mass spectrometry.
Article 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 alpha-L-threo-hex-4-enepyranosyluronate-(1-->3)-2-acetamido-2-deoxy-alpha,beta-D-glucopyranoside as determined by 1H NMR spectroscopy and MALDITOF mass spectrometry.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4112367 | PMC |
| http://dx.doi.org/10.1016/j.carres.2005.07.016 | DOI Listing |
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