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Title: Isolation of streptococcal hyaluronate synthase. Author: Prehm P, Mausolf A. Journal: Biochem J; 1986 May 01; 235(3):887-9. PubMed ID: 3092808. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]