• 1 January 1979
    • journal article
    • research article
    • Vol. 94  (4) , 532-541
Abstract
Ig[immunoglobulin]G [human] adsorbed to negatively charged crystals of monosodium urate monohydrate was restricted to cationic species of Ig. Similar binding of smaller amounts of IgG was observed with crystals other than monosodium urate monohydrate. Heated monosodium urate monohydrate and amorphous sodium urate adsorbed greater amounts of IgG and other proteins. Complement [C] activation as measured by electrophoretic conversion of C3, was not related to the amount of IgG adsorbed by the crystals studied. C1q was also adsorbed to some degree by all crystals studied but did not correlate with complement activation. [The possible importance of IgG and C in urate associated inflammation was discussed.].