The hyaluronate synthase complex was identified in plasma membranes from B6 cells. It contained two subunits of molecular masses 52 kDa and 60 kDa which bound the precursor UDP-GlcA in digitonin solution and partitioned into the aqueous phase, together with nascent hyaluronate upon Triton X-114 phase separation. The 52 kDa protein cross-reacted with poly- and monoclonal antibodies raised against the streptococcal hyaluronate synthase and the 60 kDa protein was recognized by monoclonal antibodies raised against a hyaluronate receptor. The 52 kDa protein was purified to homogeneity by affinity chromatography with monoclonal anti-hyaluronate synthase.
Research Article|March 15 1993
The hyaluronate synthase from a eukaryotic cell line
E A Turley;
Biochem J (1993) 290 (3): 791-795.
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L Klewes, E A Turley, P Prehm; The hyaluronate synthase from a eukaryotic cell line. Biochem J 15 March 1993; 290 (3): 791–795. doi: https://doi.org/10.1042/bj2900791
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