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

Jen P. Chang, Douglas E. Kiehl, Allison S. Kennington

Rapid Communications in Mass Spectrometry · 1997 · 27 citations · 0 references

Concepts

Abstract

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.