PURIFICATION AND CHARACTERISATION OF PHOSPHORYLASE FROM MUSCLE OF TILAPIA(TILAPIA MOSAMBICA)

Abstract

Phosphorylase from muscle of tilapia (Tilapia mosambica)
was extracted by water and purified by ammonium sulphate
precipitation, centrifugation and repeated recrystallisation. Electrcphorogram
of the enzyme preparation shovved a single band
near o~igin. The enzyme showed optimum pH and temperature
at 6.1 and 37°C respectively. Glucose and glucose-6-phosphate
were found to be competitive inhibitors of the enzyme. Maltose
and starch acted as primers for the phosphorylase reaction
like glycogen.02