Separation and characterization of the tryptic peptide mapping of recombinant bovine growth hormone by reversed-phase high-performance liquid chromatography electrospray mass spectrometry.

Reversed phase high-performance liquid chromatography (RPHPLC) coupled with electrospray ionization mass spectrometry (ESI-MS) was used to separate and characterize the peptides resulting from the tryptic cleavage of somidobove, a recombinant bovine growth hormone. The tryptic digestion of somidobove was carried out at room temperature for 15 hours. The tryptic peptides were separated on a Zorbax SB300 C8 column with trifluoroacetic acid--acetonitrile gradient elution and characterized by LC/ESI-MS. Resulting single and combined peptide fragments were characterized by comparing the observed molecular mass with the calculated mass for these fragments.