An electrophophoretic study on proteins of skeleton muscle of Micropogonias furnieri (Desmarest, 1823) from SE-S coast of Brasil: 1. Some technical considerations

Abstract

Effects of different positions of sampling and different periods of preservation of the samples at -15ºC on the general protein electropherograms of skeletic muscle ofMicropogpnias furnieri, were analysed and the conditions of extraction and electrophoresis of the proteins were established. Extraction and preservation powers of four solutions, distilled water, sodium chloride 0.9%, phosphate buffer pH 7,5 µ=0.05 (Connelly 1953) and glycerol-EDTA-Tris pH 8.7. (Scopes, 1968), were compared. The electrophoresis conditions were investigated using cellulose acetate membranes with six different buffer systems and starch gel with three different buffer systems. Samples of muscle collected from different positions did not show differences either in the number of bands or in their relative migrations in the electropherograms. Alterations in the electropherograms were noted according the period of sample preservation. The greatest extraction and preservation powers were found with the solution glyeerol-EDTA-tris pH 8.7. In the buffer systems used, the maximum number of nine bands was obtained in cellulose acetate membranes as well as in starch gel. The best separation of the proteins in cellulose acetate membranes was found with Tris-glyeine buffer pH 8.3 (Tris 0.0495M, glycine 0.3836M), and in starch gel with gel buffer constituted by Tris, EDTA and boric acid, pE 8.6 (Huehns, 1968) and electrode buffer constituted by boric acid and sodium hydroxid (Smithies, 1955).