Marcel Tabak

• Abstract

  Giant extracellular hemoglobin of the annelid Glossoscolex paulistus (HbGp) presents a minimum molecular mass of 3.1 MDa, and is organized as an oligomeric protein displaying a hexagonal bilayer. It consists of 144 globin, heme-containing, chains and 36 non-heme chains (linkers), presenting a high cooperativity of oxygen binding, a high oligomeric stability and a significant capacity of r…

  Structural characterization, thermal stability and chemical compounds effects in the giant extracellullar hemoglobin of Glossoscolex paulistus (HbGp), AP.R
• Small angle x-ray scattering (saxs) study of the extracellular hemoglobin of glossoscolex paulistus: effect of ph, iron oxidation..., PUB.ART
• Interaction of dipyridamole with anionic phospholipid vesicles fluorescence studies., AR.EXT

(Only some records are available in English at this moment)

• Abstract

  Glossoscolex paulistus hemoglobin (HbGp) has a molecular mass of 3.6 MDa, determined by analytical ultracentrifugation (AUC). HbGp presents high oligomeric stability, resistance to oxidation and affinity to oxygen binding. The quaternary structure of this macromolecule consists of 144 globin chains, and 36 additional chains, lacking the heme group, named linkers, organized in a double-lay…

  Biophysical and structural studies of extracellular hemoglobin of Glossoscolex paulistus, and its monomer d and dodecamer (abcd)3 subunits., BP.PD

• Abstract

  The extracellular hemoglobin of Glossoscolex paulistus (HbGp) has an extraordinary molecular mass of 3.6 MDa, with its oligomeric structure arranged as two superposed hexagonal discs forming a "bracelet". The quaternary structure of HbGp has 144 globin chains and 36 non-globin chains (named linkers). The HbGp dissociates in alkaline pH and in the presence of high surfactant concentrations…

  Thermal and kinetic stability of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp): effects of surfactants, salts, urea, iron heme oxidation state and pH., BP.PD

• Abstract

  Extracellular hemoglobin from Glossoscolex paulistus (HbGp) annelid is a gianthemoglobin, presenting a molecular mass of 3,6 x 106 Da. HbGp oligomeric structure is constituted by a hexagonal bilayer, and its dissociation leads to the formation of 1/12 of the whole native protein. Due to its extracellular nature and high resistance to auto-oxidation, as compared to vertebrate hemoglobins, …

  Analysis of giant extracellular hemoglobin from Glossoscolex paulistus (HbGp) and ionic surfactants interaction by isothermal titration calorimetry, BP.PD

(Only some records are available in English at this moment)