BEATRIZ ELANE DE ALMEIDA
11 resultados
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Resumo IPEN-doc 20256 Effects of butyrate and manganese on productivity, sialylation, N-glycosylation site occupancy and biological properties of CHO-derived thyrotropin2014 - DAMIANI, RENATA; OLIVEIRA, JOAO E.; ALMEIDA, BEATRIZ E.; SANT'ANA, PATRICIA M.; DALMORA, SERGIO L.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.Resumo IPEN-doc 16441 Glycosylation and pharmacokinetics of human thyrotropin2011 - DAMIANI, R.; OLIVEIRA, J.E.; ALMEIDA, B.E.; VORAUER-UHL, K.; BARTOLINI, P.; RIBELA, M.T.C.P.Resumo IPEN-doc 16160 Charge isomer distribution of different pituitary and recombinant human thyrotropin (hTSH) preparations2010 - DAMIANI, R.; OLIVEIRA, J.E.; ALMEIDA, B.E.; BARTOLINI, P.; RIBELA, M.T.C.P.Resumo IPEN-doc 18702 Sodium butyrate greatly enhances human thyrotropin (hTSH) synthesis by serum-free CHO cell culture with alterations of the carbohydrate moiety2012 - DAMIANI, R.; OLIVEIRA, J.E.; ALMEIDA, B.E.; BARTOLINI, P.; RIBELA, M.T.C.P.Resumo IPEN-doc 18703 Quantitative analysis of different preparations of human thyrotropin (hTSH): a comparison between RP-HPLC and the in vivo bioassay based on thyroxine stimulaton mice2012 - ALMEIDA, B.E.; DAMIANI, R.; OLIVEIRA, J.E.; RIBELA, M.T.C.P.; BARTOLINI, P.Resumo IPEN-doc 12451 Physico-chemical characterization of alpha and beta subunit of recombinant human glycoprotein hormones: hTSH and hLH2007 - CARVALHO, CRISTIANE M.; OLIVEIRA, JOAO E.; DAMIANI, RENATA; ALMEIDA, BEATRIZ E.; CECCHI, CLAUDIA R.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.Resumo IPEN-doc 14160 Indentity and integraty of 'alfa' and 'beta' - subunit of human thyrotropin prepared by prolonged acetic acid treatment2009 - ALMEIDA, BEATRIZ E.; CARVALHO, CRISTIANE M.; DAMIANI, RENATA; OLIVEIRA, JOAO E.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.Alpha- and beta- subunits, prepared by efficiently dissociating, during 16 hours, a recombinant thyrotropin (hTSH) preparation with 0.4 M acetic acid and isolating them by RP-HPLC, were analysed for what concerns their identity and integrity. Identity was evaluated by MALDI-TOF mass spectrometry (MALDI-TOF MS). A relative molecular mass of 14021 and of 15851 was obtained for a-hTSH and (3-hTSH respectively. These values agree with those obtained by analyzing the preparation before dissociation, a difference of -1.8% for a and +1.3% for (3 being observed. Integrity of the subunits was evaluated by their capacity of self reassembling and of restoring the in vivo bioactivity of the hormone. When a-hTSH and I3-hTSH subunits were incubated together in 0.2 M sodium phosphate buffer, pH 7.0, at 25°C and under gentle shaking, a complete reassociation occurred after 4 days, forming an heterodimer. In an in vivo mouse bioassay, the T4 levels of the animals treated with the reassociated hormone were non-significantly different (p> 0.05) from those obtained when the original preparation was administered (2.71± 0.63 pg/dL versus 2.84± 0.23 pg/dL, n=6, respectively). In conclusion, subunits prepared by prolonged acetic acid treatment maintain their original molecular mass and can perfectly restore the biological activity of the reassociated heterodimers.Resumo IPEN-doc 14161 Comparison between CHO-derived thyrotropin containing 'alfa' 2,6 sialic acid linkages (hlsr-hTSH) and the conventional recombinant product2009 - DAMIANI, RENATA; OLIVEIRA, JOAO E. de; ALMEIDA, BEATRIZ E.; BARTOLINI, PAOLO; RIBELA, MARIA T.C.P.Artigo IPEN-doc 20113 Reversed-phase performance liquid chromatography as an alternative to animal bioassay for human thyrotropin potency determination2014 - ALMEIDA, B.E.; DAMIANI, R.; OLIVEIRA, J.E.; DALMORA, S.L.; TORJESEN, P.A.; BARTOLINI, P.; RIBELA, M.T.C.P.Artigo IPEN-doc 13827 Efficient isolation of the subunits of recombinant and pituitary glycoprotein2009 - CARVALHO, C.M.; OLIVEIRA, J.E.; ALMEIDA, B.E.; UEDA, E.K.M.; TORJESEN, P.A.; BARTOLINI, P.; RIBELA, M.T.C.P.