B Rutigliano

Publications (6)15.47 Total impact

• Source

  Available from: jbc.org

  Article: Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi.

  R D'Avino, C Caruso, M Tamburrini, M Romano, B Rutigliano, P Polverino de Laureto, L Camardella, V Carratore, G di Prisco
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  ABSTRACT: Antarctic fish of the family Nototheniidae usually have a single major hemoglobin (Hb 1), often a second, minor component (Hb 2, about 5% of the total), and traces of another component (Hb C, less than 1%). These are functionally similar Bohr and Root effect hemoglobins. All species of other highly endemic fish families so far investigated also have one single major hemoglobin. The hematological features of the nototheniid Trematomus newnesi are remarkably different. It is the only Antarctic species in which Hb 1 and Hb 2 display only a very weak Bohr effect and no Root effect. Perhaps consequentially, Hb C (the only component showing regulation of oxygen binding by protons and other effectors) is not present in traces but accounts for 20-25% of the total. The primary structure of the three hemoglobins of T. newnesi and of Root effect HbC present in trace amounts in another nototheniid (Pagothenia bernacchii) is discussed in relationship with oxygen binding and in terms of molecular and stereochemical models. The hemoglobin multiplicity, the oxygen binding features of Hb 1 and Hb 2, and the presence of functionally distinct components, thus reveal that the oxygen transport of T. newnesi has unique characteristics.
  Journal of Biological Chemistry 05/1994; 269(13):9675-81. · 4.77 Impact Factor
• Article: The amino acid sequence of the single hemoglobin of the high-antarctic fish Bathydraco marri Norman.

  C Caruso, B Rutigliano, A Riccio, A Kunzmann, G di Prisco
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  ABSTRACT: 1. Bathydraco marri Norman is a cold-adapted Antarctic teleost (Family: Bathydraconidae), living preferably at depths between 400 and 1200 m. 2. The blood of this species contains a single hemoglobin, in which oxygen binding is pH-regulated (Bohr and Root effects). 3. The complete amino acid sequence of the alpha and beta chains of the hemoglobin of B. marri has been elucidated.
  Comparative biochemistry and physiology. B, Comparative biochemistry 09/1992; 102(4):941-6.
• Article: Hemoglobin from the antarctic fish Notothenia coriiceps neglecta. Amino acid sequence of the beta chain.

  R D'Avino, C Caruso, M E Schinina, B Rutigliano, M Romano, L Camardella, F Bossa, D Barra, G di Prisco
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  ABSTRACT: 1. Notothenia coriiceps neglecta is a cold-adapted notothenioid teleost, widely distributed in the Antarctic waters. 2. In comparison with fishes from temperate waters, the blood of this teleost contains a reduced number of erythrocytes and concentration of hemoglobin; the erythrocytes contain two hemoglobins, Hb1 and Hb2, respectively accounting for approximately 90, and 5% of the total. 3. The two components differ by the alpha chain; the amino acid sequence of the beta chain in common to the two hemoglobins has been established, thus completing the elucidation of the primary structure of the major component Hb 1.
  Comparative biochemistry and physiology. B, Comparative biochemistry 02/1990; 96(2):367-73.
• Article: The amino acid sequence of the alpha- and beta-chains of the two hemoglobins of the Antarctic fish Notothenia coriiceps neglecta.

  R D'Avino, C Caruso, M E Schininà, B Rutigliano, M Romano, L Camardella, F Bossa, D Barra, G di Prisco
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  ABSTRACT: The blood of the Antarctic fish Notothenia coriiceps neglecta contains two hemoglobins, Hb 1 and Hb 2, which have a beta-chain in common. We have elucidated the primary structure of the beta-chain (146 residues) and of the alpha-chains (142 residues) of the two hemoglobins. The two alpha-chains differ from each other by 51 residues; in comparison with globin sequences of temperate fishes, the alpha-chain of Hb 1 is more similar to that of bluefin tuna than to the alpha-chain of Hb 2 of the same species.
  FEBS Letters 07/1989; 250(1):53-6. · 3.54 Impact Factor
• Article: Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. 2. Amino acid sequence of the alpha chain of Hb1.

  R D'Avino, C Caruso, M Romano, L Camardella, B Rutigliano, G Di Prisco
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  ABSTRACT: The complete amino acid sequence of the alpha chain of the main hemoglobin of the Antarctic fish Notothenia coriiceps neglecta (family Nototheniidae) has been determined. It consists of 142 residues; an acetylated seryl residue is at the amino terminal. The molecular mass is 15,519 Da. In comparison with alpha-chain sequences of non-Antarctic poikilothermic fish hemoglobins, the homology appears to be significantly lower than that existing among the latter species. A higher homology has been found with the alpha-chain sequence of the non-poikilothermic bluefin tuna.
  European Journal of Biochemistry 03/1989; 179(3):707-13. · 3.58 Impact Factor
• Article: Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate.

  L Camardella, C Caruso, B Rutigliano, M Romano, G Di Prisco, F Descalzi-Cancedda
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  ABSTRACT: Human erythrocyte glucose-6-phosphate dehydrogenase contains a reactive lysyl residue, which can be labelled with pyridoxal 5'-phosphate. The binding of one mole of pyridoxal 5'-phosphate per mole of enzyme subunit produces substantial inactivation. The substrate glucose-6-phosphate prevents the loss of activity, suggesting that the reaction site is close to the substrate-binding site. A tryptic peptide containing the pyridoxal-5'-phosphate-binding lysyl residue has been isolated and characterised. The reactive lysyl residue has been identified in the glucose-6-phosphate dehydrogenase amino acid sequence. Comparison with glucose-6-phosphate dehydrogenase from other sources shows a high homology with a peptide containing a reactive lysyl residue, isolated from the enzyme from Saccharomyces cerevisiae; glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides also contains a region highly homologous with the sequence around the reactive lysyl residue in the human enzyme. The results of this communication provide the first direct evidence for the association of an essential catalytic function with a specific region of the molecule of human erythrocyte glucose-6-phosphate dehydrogenase.
  European Journal of Biochemistry 03/1988; 171(3):485-9. · 3.58 Impact Factor