Study on the quality of recombinant proteins using matrix-assisted laser desorption ionization time of flight mass spectrometry

摘要

AIM To study the possibility of matrix-assistedlaser desorption/ionization time of flight massspectrometry (MALDI--TOF MS) for controllingthe quality of recombinant proteins.METHODS By using MALDI--TOF MS, themoleCular weights and purity of recombinantbioactive proteins were analyzed.RESULTS The molecular weights and puritywere obtained in nine recombinant bioactiveproteins, including interleukin 2, tumor necrosisfactor Q, granulocyte--macrophage colonystimulating factor, interferon aZb, interferon al,erythropoietin, calmodulin and its fragment, andneuronal nitric oxide synthase were obtained.MALDI--TOF MS was also used to assay specificproteins in the mixtures and to characterize theerythropoietin tryptic digests.CONCLUSION The results showed that MALDITOF MS can be employed for the effective qualitycontrol of recombinant proteins.