Lo studio approfondisce le nostre conoscenze sull'uso alimentare del pesce in Etruria prevalentemente grazie a fonti letterarie e archeologiche (resti paleozoologici, reperti archeologici connessi con la pesca, dossier iconografici presenti su varie classi di documenti archeologici), e, laddove carenti, grazie a quanto documentato in Grecia negli stessi periodi storici. Ampie sezioni sono dedicate al rapporto tra gli Etruschi e il mare (fonti letterarie, i porti, le imbarcazioni da pesca, la musica che attira i pesci, la pesca del tonno, raffigurazioni di pesci, i naufragi, le tecniche di pesca utilizzate cioè con la lenza e la canna, con la rete, con la fiocina o tridente, con la nassa, con vasi dall'imboccatura stretta), all'analisi della filiera della pesca (trasporto, preparazione e conservazione cottura e consumo del pesce) e agli usi del pesce nel culto (offerta di pesce per i defunti e per gli dei). Una specifica sezione è dedicata ai "piatti da pesce", una classe di piatti che recano la raffigurazione di pesci nella tecnica a figure rosse, prodotta anche in Etruria meridionale (a Cerveteri). Chiudono lo studio alcune considerazioni sul commercio del pesce dai porti dell'Etruria meridionale (Pyrgi in primis) sul Tirreno verso l'interno della regione.

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-á(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.

The Gymnothorax unicolor hemoglobin system is characterized by two components, called cathodic and anodic on the basis of their isoelectric point, which were separated by ion-exchange chromatography. The oxygen-binding properties of the purified components were studied in the absence and presence of chloride and/or GTP or ATP in the pH range 6.5-8.0. Stripped cathodic hemoglobin showed a small reverse Bohr effect, high oxygen affinity, and low co-operativity; the addition of chloride only caused a small decrease in oxygen affinity. In the presence of GTP or ATP, the oxygen affinity was dramatically reduced, the co-operativity increased, and the reverse Bohr effect abolished. Stripped anodic hemoglobin is characterized by both low oxygen affinity and co-operativity, and displayed a normal Bohr effect; the addition of chloride increased co-operativity, whereas ATP and GTP significantly modulated oxygen affinity at acidic pH values, enhancing the Bohr effect and giving rise to the Root effect. The complete amino-acid sequences of the alpha and beta chains of both hemoglobins were established; the molecular basis of the functional properties of the hemoglobins is discussed in the light of the primary structure and compared with those of other fish hemoglobins.