Pichia pastoris cells transformed with a plasmid engineered for the expression of tilapia
growth hormone as a secreted product produced a proteolytically cleaved form of the
recombinant protein. The sequence of this truncated variant was obtained by mass
spectrometry analysis. The cleavage site was determined to be between residues Tyr 158
and Tyr 159. The resulting truncated tilapia growth hormone was a single chain protein
lacking 46 amino acids of the C-terminal portion. In this study, we showed that the truncated …