ELIZABETH KINUYO GIMBO VIANNA

ELIZABETH KINUYO GIMBO VIANNA

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Reversed-phase high-performance liquid chromatography method for the determination of prolactin in bacterial extracts and in its purified form
2002 - SOARES, C.R.J.; CAMARGO, I.M.C.; MORGANTI, L.; VIANNA, E.K.G.; OLIVEIRA, J.E.; LEGOUX, R.; FERRARA, P.; BARTOLINI, P.
Analysis of recombinant human growth hormone directly in osmotic shock fluids
1997 - DALMORA, S.; OLIVEIRA, J.E.; AFFONSO, R.; GIMBO VIANNA, E.K.; RIBELA, M.T.C.P.; BARTOLINI, P.
High-yield purification of biosynthetic human growth hormone secreted in Escherichia coli periplasmic space
1999 - OLIVEIRA, J.E.; SOARES, C.R.J.; PERONI, C.N.; VIANNA, E.K.G.; CAMARGO, I.M.C.; MORGANTI, L.; BELLINI, M.H.; AFFONSO, R.; ARKATEN, R.R.; BARTOLINI, P.; RIBELA, M.T.C.P.
High-level expression of human thyroid-stimulating hormone in Chinese hamster ovary cells by co-transfection of dicistronic expression vectors followed by a dual-marker amplification strategy
2002 - PERONI, C.N.; SOARES, C.R.J.; VIANNA, E.K.G.; MORGANTI, L.; RIBELA, M.T.C.P.; BARTOLINI, P.
Stable expression of a human-like sialylated recombinant thyrotropin in a Chinese hamster ovary cell line expressing α2,6-sialyltransferase
2009 - DAMIANI, RENATA; OLIVEIRA, JOAO E.; VORAUER-UHL, KAROLA; PERONI, CIBELE N.; VIANNA, ELIZABETH G.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.
A CHO cell line, previously genetically modified by the introduction of rat α2,6-sialyltransferase cDNA, generated for the first time a human-like sialylated recombinant hTSH (hlsr-hTSH) more similar to the native hormone, with 61% of α2,3- and 39% of α2,6-linked sialic acid residues. The best clone, when submitted to gene amplification with up to 8 μM methotrexate, presented a secretion level of ∼2 μg hTSH/106 cells/day, useful for product purification and characterization. The relative molecular masses (Mr) of the heterodimer and of the α- and β-subunits of purified hlsr-hTSH, determined by MALDI-TOF mass spectrometry, and the relative hydrophobicities, determined by RP-HPLC, were not remarkably different from those presented by two r-hTSH preparations secreted by normal CHO cells. Some differences were observed, though, in N-glycan composition, with more tri- and much more tetra-sialylated structures in hlsr-hTSH. When analyzed via an in vivo bioassay based on hTSH-induced T4 release in mice, hlsr-hTSH was shown to be equipotent (p > 0.05) with the commercial preparation of r-hTSH (Thyrogen), and 1.6-fold more potent than native hTSH (p < 0.001).