| Literature DB >> 8457208 |
L Klewes1, E A Turley, P Prehm.
Abstract
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.Entities:
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Year: 1993 PMID: 8457208 PMCID: PMC1132350 DOI: 10.1042/bj2900791
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857