Abstract

The yellowspotted puffer (Torquigener flavimaculosus, Hardy & Randall, 1983 samples were collected in Fethiye Bay, Turkey. Gel electrophoresis is a separation technique which is often used to separate large molecules such as proteins. Thus, the size of the polypeptide chains of a given protein can be determined by comparing their electrophoretic mobilities on SDS gels to the mobilities of marker proteins with well-characterized polypeptide chain molecular weights. In this study, tricholoracetic acid (TCA)-acetone precipitated proteins of muscle and liver of yellowspotted puffer was separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The pufferfish muscle proteins resolved molecular mass range of 6.500−200.000 kDa for muscle and 6.500-116.250 kDa for liver, following Comassie blue staining.