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

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.

AIM:To study the possibility of matrix-assisted laser esorption/ionization time of flight mass spectrometry (MALDI-TOF MS) for controlling the quality of recombinant proteins.METHODS:By using MALDI-TOF MS, the molecular weights and purity of recombinant bioactive proteins were analyzed.RESULTS:The molecular weights and purity were obtained in nine recombinant bioactive proteins, including interleukin 2,tumor necrosis factor alpha, granulocyte macrophage colony stimulating factor, interferon alpha2b, interferon alpha1, erythropoietin, calmodulin and its fragment, and neuronal nitric oxide synthase were obtained. MALDI-TOF MS was also used to assay specific proteins in the mixtures and to characterize the erythropoietin tryptic digests.CONCLUSION:The results showed that MALDI-TOF MS can be employed for the effective quality control of recombinant proteins.