Abstract
Sera from a number of different species were found to contain a hyaluronate binding activity. This binding activity was detected by mixing the serum with [ 3 H] hyaluronate and then precipitating the proteins and any bound [ 3 H] hyaluronate by the addition of an equal volume of saturated (NH 4 ) 2 SO 4 . The binding activity associated with horse serum was examined further and found to be saturable, of relatively high affinity and specific for hyaluronate. Competition experiments showed that the binding was not influenced by the molecular weight of the hyaluronate, suggesting that the binding protein interacts with an intrachain region of the hyaluronate rather than the terminals. The binding activity co-purified with the IgG and IgM fractions of serum after (NH 4 ) 2 SO 4 precipitation, ion-exchange and molecular-sieve chromatography as well as after affinity chromatography.
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