Open AccessStudy on the quality of recombinant proteins using matrix-assisted laser desorption ionization time of flight mass spectrometry
Author(s) -
Guohua Zhou
Publication year - 1999
Publication title -
world journal of gastroenterology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.427
H-Index - 155
eISSN - 2219-2840
pISSN - 1007-9327
DOI - 10.3748/wjg.v5.i3.235
Subject(s) - recombinant dna , mass spectrometry , chemistry , time of flight mass spectrometry , matrix assisted laser desorption/ionization , chromatography , erythropoietin , molecular mass , matrix (chemical analysis) , microbiology and biotechnology , desorption , biochemistry , ionization , biology , enzyme , ion , organic chemistry , adsorption , gene , endocrinology
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.