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Isolation of streptococcal hyaluronate synthase.

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.

SUBMITTER: Prehm P

PROVIDER: S-EPMC1146770 | biostudies-other | 1986 May

REPOSITORIES: biostudies-other

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Shedding of hyaluronate synthase from streptococci.

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Streptococcal species

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