Isolation of streptococcal hyaluronate synthase.
Hyaluronate synthase was isolated from protoblast membranes of streptococci by Triton X-114 extraction and cetylpyridinium chloride precipitation. It was identified as a 52,000-Mr protein, which bound to nascent hyaluronate and was affinity-labelled by periodate-oxidized UDP-glucuronic acid and UDP-N-acetylglucosamine. Antibodies directed against the 52,000-Mr protein inhibited hyaluronate synthesis. Mutants defective in hyaluronate synthase activity lacked the 52,000-Mr protein in membrane extracts. Synthase activity was solubilized from membranes by cholate in active form and purified by ion-exchange chromatography.
D001426:Bacterial Proteins / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D014453:Glucuronosyltransferase / Q000276:immunology / Q000302:isolation & purification*; D016695:Glycosyltransferases; D000076002:Hyaluronan Synthases; D008565:Membrane Proteins / Q000302:isolation & purification; D013291:Streptococcus / Q000201:enzymology*; D014166:Transferases; D029867:Xenopus Proteins
D001426:Bacterial Proteins; D008565:Membrane Proteins; D029867:Xenopus Proteins; D014166:Transferases; D016695:Glycosyltransferases; D014453:Glucuronosyltransferase; C056944:HAS1 protein, Xenopus; D000076002:Hyaluronan Synthases