Control of enzymatic degradation of hyaluronan by divalent cations. |
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| Authors: | K P Vercruysse M R Ziebell G D Prestwich |
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| Affiliation: | University of Utah, Department of Medicinal Chemistry, Salt Lake City 84112-5820, USA. |
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| Abstract: | Enzymatic degradation of hyaluronan (HA) by testicular hyaluronidase (HAase, hyaluronate 4-glucanohydrolase) requires inclusion of mono- or divalent cations in the reaction mixture. Most divalent cations activated HAase with equal potency; however, Cu2+ suppressed degradation, and Ca2+ showed a concentration-dependent regulation of size of the oligosaccharide products. Careful selection of HAase assay parameters is critical for discovery of novel HAase inhibitors and for preparation of controlled-size oligosaccharide fragments. |
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