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• W1987632841 abstract "In the present study we describe a method to prepare membranes with high hyaluronan synthase activity from human glioma cells by pretreatment of the cells with both testicular hyaluronidase and 4-phorbol 12-myristate 13-acetate (PMA). A 23-fold increase in hyaluronan synthase activity was detected in comparison to untreated cells. Using isolated membranes as a source of hyaluronan synthase activity we demonstrate that chain elongation occurs at the reducing end of the hyaluronan molecule. We also present a method to solubilize hyaluronan synthase in active form with 1% digitonin. The solubilized synthase synthesized shorter hyaluronan chains than the membrane bound enzyme. Partial purification of the solubilized enzyme on a Superdex-200 column revealed a 12-fold increase in specific activity. Affinity purified polyclonal antibodies, raised against a synthetic peptide corresponding to the carboxy-terminus of the deduced protein sequence of human hyaluronan synthase recognized a 66 kDa component in the purified preparations. The elution position of the solubilized hyaluronan synthesizing activity immediately after V0 corresponding to a molecular mass of about 600 kDa, suggested that the 66 kDa enzyme forms a complex with other components which may have accessory or regulatory roles during hyaluronan synthesis." @default.
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• W1987632841 date "1998-05-01" @default.
• W1987632841 modified "2023-09-27" @default.
• W1987632841 title "Characterization of hyaluronan synthase from a human glioma cell line" @default.
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• W1987632841 doi "https://doi.org/10.1016/s0304-4165(98)00010-5" @default.
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