On the molecular mass of the extracellular hemoglobin of Glossoscolex paulistus: Analytical ultracentrifugation reexamination

Carvalho, Francisco Adriano de Oliveira; Santiago, Patrícia S.; Borges, Júlio César; Tabak, Marcel

doi:10.1016/j.ab.2008.11.008

Cited by 31 publications

(34 citation statements)

References 37 publications

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“…The obtained values of 3.6 ± 0.1 MDa and 3.7 ± 0.1 MDa, respectively, for the two forms are in good agreement with the value of M estimated from mass spectrometric data as mentioned above and considering the Vinogradov model [11]. In the present work, AUC data are analyzed for HbGp in the same two oxidation states as described in [18], for alkaline protein solutions at pH 10.0. This pH value is known to produce extensive oligomeric dissociation for HbGp [9,19,20].…”

Section: Introductionsupporting

confidence: 76%

“…In a recent work [18] the determination of M was performed for two samples of HbGp, in the oxy-and cyanomet-forms, at pH 7.0, where the protein is very stable. The obtained values of 3.6 ± 0.1 MDa and 3.7 ± 0.1 MDa, respectively, for the two forms are in good agreement with the value of M estimated from mass spectrometric data as mentioned above and considering the Vinogradov model [11].…”

Section: Introductionmentioning

confidence: 99%

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Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: Alkaline oligomeric dissociation

Carvalho

Santiago

Borges

et al. 2011

International Journal of Biological Macromolecules

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Section: Introductionsupporting

confidence: 76%

Section: Introductionmentioning

confidence: 99%

Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: Alkaline oligomeric dissociation

Carvalho

Santiago

Borges

et al. 2011

International Journal of Biological Macromolecules

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“…1,2 Extracellular hemoglobin of Glossoscolex paulistus (HbGp) is an erythrocruorin that shows a molecular mass of 3.6 MDa, determined by analytical ultracentrifugation. 3 HbGp has a hexagonal bilayer oligomeric structure composed by 144 globin chains and 36 additional chains lacking the heme group, named linkers. 4 It is constituted by twelve protomers, formed by a dodecamer (abcd) 3 of globin chains and a trimer of linkers L 1 L 2 L 3 .…”

Section: Introductionmentioning

confidence: 99%

“…3 HbGp has a hexagonal bilayer oligomeric structure composed by 144 globin chains and 36 additional chains lacking the heme group, named linkers. 4 It is constituted by twelve protomers, formed by a dodecamer (abcd) 3 of globin chains and a trimer of linkers L 1 L 2 L 3 . The dodecamer is composed of three asymmetric tetramers abcd constituted by a disulfide bonded trimer abc and a monomer subunit d, and the linkers L 1 , L 2 , and L 3 complete the protomer structure.…”

Section: Introductionmentioning

confidence: 99%

Interaction of cationic dodecyl‐trimethyl‐ammonium bromide with oxy‐HbGp by isothermal titration and differential scanning calorimetric studies: Effect of proximity of isoelectric point

Alves

Carvalho

et al. 2016

Biopolymers

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In this work, isothermal titration and differential scanning calorimetric methods, in combination with pyrene fluorescence emission and dynamic light scattering have been used to investigate the interaction of dodecyltrimethylammonium bromide (DTAB) with the giant extracellular Glossoscolex paulistus hemoglobin (HbGp) in the oxy-form, at pH values around the isoelectric point (pI ≈ 5.5). Our ITC results have shown that the interaction of DTAB with the hemoglobin is more intense at pH 7.0, with a smaller cac (critical aggregation concentration) value. The increase of protein concentration does not influence the cac value of the interaction, at both pH values. Therefore, the beginning of the DTAB-oxy-HbGp premicellar aggregates formation, in the cac region, is not affected by the increase of protein concentration. HSDSC studies show higher Tm values at pH 5.0, in the absence and presence of DTAB, when compared with pH 7.0. Furthermore, at pH 7.0, an aggregation process is observed with DTAB in the range from 0.75 to 1.5 mmol/L, noticed by the exothermic peak, and similar to that observed for pure oxy-HbGp, at pH 5.0, and in the presence of DTAB. DLS melting curves show a decrease on the hemoglobin thermal stability for the oxy-HbGp-DTAB mixtures and formation of larger aggregates, at pH 7.0. Our present data, together with previous results, support the observation that the protein structural changes, at pH 7.0, occur at smaller DTAB concentrations, as compared with pH 5.0, due to the acidic pI of protein that favors the oxy-HbGp-cationic surfactant interaction at neutral pH.

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“…A hemoglobina extracelular gigante de Glosscoslex paulistus (HbGp) apresenta uma estrutura oligomérica altamente organizada, composta por 144 cadeias polipeptídicas com grupo heme (globinas) e 36 cadeias polipeptídicas sem grupos heme, que são chamadas de cadeias linkers (L), com uma massa molecular total de 3,6 MDa [3][4][5]. A estrutura oligomérica da HbGp é formada por dois discos hexagonais, sobrepostos formando uma bicamada hexagonal ( Fig.…”

Section: Hemoglobina Extracelular De Glossoscolex Paulistus (Hbgp)unclassified

Estudo da estabilidade térmica da hemoglobina extracelular gigante de Glossoscolex paulistus (HbGp): efeitos do estado de oxidação do ferro do grupo heme, pH e presença de surfactante

Carvalho¹

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AgradecimentosAgradeço! Aos meus pais Maria Gorete Pires Carvalho e José de Ribamar Gomes Carvalho e a minha esposa Sumária Sousa e Silva pela dedicação, carinho, motivação nas horas mais difíceis, sem eles não teria forças para seguir essa jornada; Ao Professor Marcel Tabak por sua orientação e pelos laços de amizade e respeito que se formaram nesta convivência e também pela oportunidade de poder desenvolver esse trabalho;A Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP) pela bolsa de doutorado;Aos meus irmãos Genilson, Genilda e Gesilda pelo apoio, carinho e afeto que temos e pelas palavras amigas;Às minhas tias Eva (segunda mãe), Maria da Guia e Raimunda Teresa e os primos (as) Rita de Kássia, Karla Karolina, Raiza, Rairone, Railson, Amanda e Constância pelo apoio e carinho que sempre me motiva; Aos meus amigos de laboratório Adriano, Fernanda, Ana Eliza, Diógenes e Ezer Biazin, pelo apoio moral e pela contribuição direta e indireta na minha formação e neste trabalho. Obrigado em especial a vocês Adriano e Ezer Biazin; Aos meus amigos Orlando, Ana Célia, Adriane, Washington, Alexandre, Tairo, Adriana, Elenice, Jairo e Edvan pelas discussões bem humoradas e pela amizade; Aos professores Dr.(a) (s) Leandro R. S. Barbosa (IF-USP), Rosângela Itri (IF-USP), Patríca S. Santiago (UNESP-Registro), Carlos Ernesto Garrido Salmon (USP-Riberão Preto) e Tatiana Batista (UEL-PR) pelas discussões e colaborações durante meu curso de doutorado, que foi muito importante para minha formação; Ao Ezér Biazin, técnico do laboratório, por toda ajuda na parte instrumental e que sem nenhuma dúvida foi muito importante para o bom desenvolvimento deste trabalho e pela amizade que se construiu nestes cinco anos; A Andressa Patrícia Alves Pinto, técnica do laboratório de biofísica do IFSC por toda ajuda nos experimentos de CD que foi muito importante para o bom desenvolvimento deste trabalho; Ao Laboratório Nacional de Luz Síncrotron (LNLS), em especial ao Dr. Mateus Cardoso, coordenador da linha SAXS2, pelo auxílio na realização das medidas de SAXS;Ao pessoal da pós-graduação, Sílvia, Andréia e Gustavo, por toda a atenção, carinho e pelos bons serviços prestados;A dona Suely e seu José de Ribamar pelos conselhos e apoio nos momentos difíceis.

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On the molecular mass of the extracellular hemoglobin of Glossoscolex paulistus: Analytical ultracentrifugation reexamination

Cited by 31 publications

References 37 publications

Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: Alkaline oligomeric dissociation

Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: Alkaline oligomeric dissociation

Interaction of cationic dodecyl‐trimethyl‐ammonium bromide with oxy‐HbGp by isothermal titration and differential scanning calorimetric studies: Effect of proximity of isoelectric point

Estudo da estabilidade térmica da hemoglobina extracelular gigante de Glossoscolex paulistus (HbGp): efeitos do estado de oxidação do ferro do grupo heme, pH e presença de surfactante

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