title: Control of enzymatic degradation of hyaluronan by divalent cations.
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.
authors.affiliation: University of Utah, Department of Medicinal Chemistry, Salt Lake City 84112-5820, USA.
authors.forename: K P
authors.initials: KP
authors.lastname: Vercruysse
authors.forename: M R
authors.initials: MR
authors.lastname: Ziebell
authors.forename: G D
authors.initials: GD
authors.lastname: Prestwich
mesh_terms: D002118:Calcium / Q000494:pharmacology; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002413:Cations, Divalent / Q000494:pharmacology*; D006820:Hyaluronic Acid / Q000737:chemistry / Q000378:metabolism*; D006821:Hyaluronoglucosaminidase / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D002413:Cations, Divalent; D009844:Oligosaccharides; D006820:Hyaluronic Acid; D006821:Hyaluronoglucosaminidase; D002118:Calcium