Tryptic mapping of human chorionic gonadotropin by matrix‐assisted laser desorption/ionization mass spectrometry

Abstract

The potential of matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI)(I‐TOF) mass spectrometry for use in the identification of human chorionic gonadotropin (hCG) seized by law enforcement agencies is investigated. Analysis of untreated hCG revealed signals corresponding to the molecular ions of the intact hCG heterodimer and both its non‐covalently linked subunits. Unfortunately, due to carbohydrate heterogeneity, the peaks are broad which makes accurate mass assignment, and consequently identification, difficult. Peptide mapping by MALDI‐TOF following‐tryptic digestion gave sequence coverage of 59% and 52% for the α and b̃‐subunits respectively. Nevertheless, the tryptic map was considered to provide unambiguous identification of hCG. This was confirmed by searching peptide‐mass databases with the experimentally determined masses. Our data suggest that peptide mapping by proteolytic digestion followed by MALDI‐TOF mass spectrometry is a suitable analytical technique for the identification of hCG seized by the legal authorities.