WHOLE CELL PROTEIN PROFILING OF PASTEURELLA MULTOCIDA FIELD ISOLATES IN PAKISTAN

Eight haemorrhagic septicaemia (HS) related Pasteurella multocida isolates, collected from different localities of Pakistan, were characterized by sodium-dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) technique. After sonification, the bacterial proteins were separated by centrifugation. Proteins from sonicated supernatant were salted out by ammonium sulfate. Sonicated supernatant, as well as ammonium sulfate precipitated proteins, were analyzed. Molecular weights of proteins were determined from graph between Rf value and log of molecular weight. The ammonium sulfate treated samples showed fewer bands with low molecular weights of 54, 45, 42, 40 and 20.5 kDa, while total 31 visible bands were observed in sonicated supernatants ranging from 126 to 11 kDa. The common protein bands in both preparations were of 54 and 23 kDa molecular weight.