Electrophoretic and zymogram analysis of the cytoplasmic soluble protein fraction of Spiroplasma citri

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Abstract
The biological function of proteins in the soluble cytoplasmic fraction of two isolates of Spiroplasma citri was investigated by zymogram analysis. There were quantitative and qualitative differences in the isozyme patterns of esterase and RNase between the two isolates of S. citri. Esterase activity in S. citri, reported here for the first time, was higher in one isolate, while RNase activity was higher in the other. No activity was detected in either isolate for acid phosphatase, alkaline phosphatase, or peroxidase. Spiralin, detected in the the cytoplasmic fraction using both native and denaturing polyacrylamide gel electrophoresis, did not appear to be an isozyme of any of the enzymes tested.