Objective: Rheumatoid arthritis (RA) is an autoimmune disease where sera and synovial fluid (SF) of suffering patients contain immune complexes formed from autoantibodies to several proteins. SF from humans with joint diseases was examined for the presence of some inflammatory parameters and autoantibodies.Materials and Methods: Antibodies in their free and complex forms were assayed by indirect ELISA. The immunoprecipitation technique was used to evaluate total IgG and IgM and complement. Results:The results showed that most RA SF was anti-ASLO negative, but they were CRP positive. Levels of complement components (C3 and C4) were highest in the group of mono-/oligo-arthritis and lowest in RA. The results showed that xanthine oxidase (XO) presence and activity were important in SF of RA patients. Moreover, free and complex anti-XO antibodies were detected in all SF with different titers throughout the groups of patients where IgG was lower than IgM. Conclusion:The studied parameters of inflammation and auto-antibodies especially against XO could serve as an evaluation of the severity of joint inflammation and in RA pathogenesis understanding.

Fractionation of human plasma on ion exchanger resin was performed on Amberlite IRC-718 saturated with metal ions. Depletion of human immunoglobulin G was carried out by column chromatography using Tris-HCl, pH 7 at different concentrations. Results showed that, when Cu þ2 and Ni þ2 were adsorbed on the resin, one or two fractions of purified IgG were obtained, respectively. Whereas Fe þ2 and Zn þ2 , both retain IgG and serum albumin or serum albumin alone. Furthermore, the Ni þ2 -resin retention of serum proteins is too strong that the use of 700 mMTris-HCl cannot liberate any other proteins than nonadsorbed serum albumin. In conclusion, this investigation demonstrates that immobilized metal ion affinity chromatography with Cu 2þ , Ni 2þ , and Fe 2þ immobilized on Amberlite IRC-718 has the potential to be developed as part of a process to purify IgG out of untreated human plasma as acceptable adsorption and elution levels of IgG could be achieved.

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Definitive evidence for the discrete biological role of Prolyl Oligopeptidase (PO) remains unknown, though various physiological functions for the enzyme have been implicated. Many peptide