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40 results on '"Pellegrini, Mariagiuseppina"'

1. The Surprising Composition of the Salivary Proteome of Preterm Human Newborn

Author

Castagnola, Massimo, Inzitari, Rosanna, Fanali, Chiara, Iavarone, Federica, Vitali, Alberto, Desiderio, Claudia, Vento, Giovanni, Tirone, Chiara, Romagnoli, Costantino, Cabras, Tiziana, Manconi, Barbara, Teresa Sanna, Maria, Boi, Roberto, Pisano, Elisabetta, Olianas, Alessandra, Pellegrini, Mariagiuseppina, Nemolato, Sonia, Wilhelm Heizmann, Claus, Faa, Gavino, and Messana, Irene

Published
2011
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6. Trafficking and Postsecretory Events Responsible for the Formation of Secreted Human Salivary Peptides: A Proteomics Approach

Author

Messana, Irene, Cabras, Tiziana, Pisano, Elisabetta, Sanna, Maria Teresa, Olianas, Alessandra, Manconi, Barbara, Pellegrini, Mariagiuseppina, Paludetti, Gaetano, Scarano, Emanuele, Fiorita, Antonella, Agostino, Stefania, Contucci, Alessia M., Calò, Lea, Picciotti, Pasqualina M., Manni, Armando, Bennick, Anders, Vitali, Alberto, Fanali, Chiara, Inzitari, Rosanna, and Castagnola, Massimo

Published
2008
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22. Functional properties of the newly observed Gγ-chain fetal hemoglobin variant Hb F-Monserrato-Sassari (HBG2:c.280T>C) or [Gγ93 (F9) Cys→Arg]

Author

Pellegrini, Mariagiuseppina, primary, Manconi, Barbara, additional, Olianas, Alessandra, additional, Sanna, Maria Teresa, additional, Meloni, Claudia, additional, Pirastru, Monica, additional, Mereu, Paolo, additional, Leoni, Giovanni, additional, Masala, Bruno, additional, and Manca, Laura, additional

Published
2011
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23. Structural-functional characterisation of the cathodic haemoglobin of the conger eel, Conger conger. Molecular modelling study of an additional phosphate-binding site

Author

Pellegrini, Mariagiuseppina, Giardina, Bruno, Verde, Cinzia, Carratore, Vito, Olianas, Alessandra, Sollai, Luigi, Sanna, Maria Teresa, Castagnola, Massimo, Di Prisco, Guido, Castagnola, Massimo (ORCID:0000-0002-0959-7259), Pellegrini, Mariagiuseppina, Giardina, Bruno, Verde, Cinzia, Carratore, Vito, Olianas, Alessandra, Sollai, Luigi, Sanna, Maria Teresa, Castagnola, Massimo, Di Prisco, Guido, and Castagnola, Massimo (ORCID:0000-0002-0959-7259)

Abstract

The Conger conger (conger eel) haemoglobin (Hb) system is made of three components, one of which, the so-called cathodic Hb, representing approx. 20% of the total pigment, has been purified and characterized from both a structural and functional point of view. Stripped Hb showed a reverse Bohr effect, high oxygen affinity and slightly low cooperativity in the absence of any effector. Addition of saturating GTP strongly influences the pH dependence of the oxygen affinity, since the reverse Bohr effect, observed under stripped conditions, is converted into a small normal Bohr effect. A further investigation of the GTP effect on oxygen affinity, carried out by fitting its titration curve, demonstrated the presence of two independent binding sites. Therefore, on the basis of the amino acid sequence of the alpha- and beta-chains, which have been determined, a computer modelling study has been performed. The data suggest that C. conger cathodic Hb may bind organic phosphates at two distinct binding sites located along the central cavity of the tetramer by hydrogen bonds and/or electrostatic interactions with amino acid residues of both chains, which have been identified. Among these residues, the two Lys-alpha(G6) (where the letter refers to the haemoglobin helix and the number to the amino acid position in the helix) appear to have a key role in the GTP movement from the external binding region to the internal central cavity of the tetrameric molecule.

Published
2003

31. The hemoglobin system of the brown morayGymnothorax unicolor

Author

Tamburrini, Maurizio, primary, Verde, Cinzia, additional, Olianas, Alessandra, additional, Giardina, Bruno, additional, Corda, Marcella, additional, Sanna, Maria T., additional, Fais, Antonella, additional, Deiana, Anna M., additional, di Prisco, Guido, additional, and Pellegrini, Mariagiuseppina, additional

Published
2001
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38. Functional properties of the newly observed Gγ-chain fetal hemoglobin variant Hb F-Monserrato-Sassari (HBG2:c.280T>C) or [Gγ93 (F9) Cys→Arg]

Author

Pellegrini, Mariagiuseppina, Manconi, Barbara, Olianas, Alessandra, Sanna, Maria Teresa, Meloni, Claudia, Pirastru, Monica, Mereu, Paolo, Leoni, Giovanni, Masala, Bruno, and Manca, Laura

Subjects
*HEMOGLOBIN polymorphisms, *HEMOGLOBINOPATHY in children, *ELECTROPHORESIS, *CORD blood, *ELECTROSPRAY ionization mass spectrometry, *SARDINIANS, *GENETIC mutation, *HIGH performance liquid chromatography, *DISEASES
Abstract

Abstract: Background: HbF-Monserrato-Sassari is a newly discovered abnormal fetal hemoglobin observed in an apparently normal newborn baby during a hemoglobinopathies survey at birth in North Sardinian population. Methods: Electrophoretic analysis of the cord blood lysate evidenced for an abnormal tetramer due to a mutated fetal globin chain. Electrospray ionisation-mass spectrometry and gene sequencing were used to identify the mutation. Oxygen binding ability of the variant Hb was determined. Results: Sequencing of the γ globin genes revealed the TGT→ CGT transition at codon 93 in one of the two Gγ genes, which leads to the Arg for Cys amino acid replacement at position 9 of the F α-helix. The amino acid substitution was confirmed by mass spectrometric analysis of the globin chains. Since modifications or substitutions at position β93 are known to affect the arrangement of a salt bridge at the α1β2 sliding contacts that are crucial for subunit cooperativity, the functional properties of the variant were studied to evaluate the effect of the replacement at the same position in the γ globin chain. With respect to normal HbF, the variant showed a significant increase in oxygen affinity and a slight decrease of both Bohr effect and cooperativity. General significance: Result indicates a key role of the Cys γ93 residue for subunit cooperativity in the T→R transition of the HbF tetramer. Substitutions at the F9 position of the Gγ globin may result in stabilization of the high affinity R-state of the Hb tetramer. Because of the loss of Cys γ93 residue, this variant is considered to be potentially compromised in nitric oxide transport. [Copyright &y& Elsevier]

Published
2011
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39. Structure/function relationships in the hemoglobin components from moray (<em>Muraena helena</em>).

Author

Pellegrini, Mariagiuseppina, Giardina, Bruno, Olianas, Alessandra, Sanna, Maria Teresa, Deiana, Anna Maria, Salvadori, Susanna, Di Prisco, Guido, Tamburrini, Maurizio, and Corda, Marcella

Subjects
*HEMOGLOBINS, *BLOOD proteins, *HEMOPROTEINS, *MORAYS, *PHENOTYPES, *BIOCHEMISTRY
Abstract

Concerning the number and type of the hemoglobin components, the moray Muraena helena is characterized by three different phenotypes whose frequencies are nearly identical. Thus, the cathodal component is present in all individuals, whereas one or both of two amodal components may be present in the same phenotype. These components have been separated by chromatography. The oxygen binding properties of the purified hemoglobin components have been studied in the absence and presence of saturating concentrations of ATP or GTP and as a function of pH. The cathodal component shows an intrinsic O2 affinity four times higher than that of both anodal components, a very small Bohr effect and a significant decrease in O2 affinity upon addition of ATP and GTP (three and four times respectively with respect to stripped conditions), the latter being more effective than the former over the entire pH range examined. The anodal components do not appear functionally distinguishable and show the presence of an enhanced Bohr effect (Root effect) that is under the strict control of nucleotide triphosphates ATP, GTP, which, unlike in the cathodic component, exert the same effect on oxygen affinity. The complete sequence of the β chains of the cathodal and of one of the anodal components have been determined. The possible molecular basis of these different functional characteristics are discussed in the light of the globin sequence and of those amino acid residues which are known to be responsible of hemoglobin functional behaviour. [ABSTRACT FROM AUTHOR]

Published
1995
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40. Oxidation of meso-Diaminosuccinic Acid, a Possible Natural Substrate for D-Aspartate Oxidase.

Author

Rinaldi, Augusto, Pellegrini, Mariagiuseppina, Crifò, Carlo, and De Marco, Carlo

Subjects
*OXIDATION, *ASPARTIC acid, *DECARBOXYLATION, *DEAMINATION, *PROTEIN deamination, *PYRIDAZINES
Abstract

meso-Diaminosuccinic acid, a natural antagonist of aspartic acid, is a good substrate for beef kidney D-aspartate oxidase. The oxygen consumption and the ammonia production are in good agreement with the stoichiometry of a typical oxidative deamination, The deamination involves only one of the two amino groups of diaminosuccinate, and is followed by decarboxylation of the first reaction product, 2-amino-3-oxosuccinic acid. By condensation of the compounds thus originating from this latter, pyrazine 2,5-dicarboxylic acid and pyrazine 2,6-dicarboxylic acid are formed, DL-Diaminosuccinic acid is not oxidized by D-spartate oxidase, nor does it inhibit the enzyme activity. [ABSTRACT FROM AUTHOR]

Published
1981
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