ABSTRACT
In this study, ten samples of synovial fluid were aspirated from normal as well as another ten rheumatoid samples. Proteoglycans were extracted from synovial fluids, then purified by gel chromatography. The results showed that there was an alteration in the structure of rheumatoid arthritic proteoglycans. The molecular weight was lower in rheumatoid proteoglycans as shown from the elution volume of the isolated proteoglycans. A shift and a decrement in the absorbance peak of proteoglycans absorption spectrum were observed. Moreover, there was an alteration in the bands number of high voltage electrophoresis. Fractions separated from normal and rheumatoid proteoglycans had the same number, but they were different in contents. Furthermore, a significant difference in amino acid contents between the two groups was detected, this alteration was suggested to be due to either the enzymatic activity or the alteration in m-RNA