The annual Congress of the Italian Biochemical and Molecular Biology Society (SIB) was held in September 1999 in Alghero, Sardegna, Italy. The programme envisaged a symposium on molecular adaptations of haemoglobin function in ver­ tebrates. Haemoglobin specialists from several countries were invited to speak at the symposium and paved the way for wide-ranging and stimulating discussions. The symposium contributions have been collected together in this volume. The structure/function relationship in haemoglobins from vertebrates (fishes populat­ ing temperate and polar environments, diving birds, marine and terrestrial mam­ mals) has been tackled from many angles, focusing on the adaptation of the oxy­ gen-transport system to the constraints dictated by the environment. Eleven arti­ cles review some of the most recent developments of the studies on this ancient oxygen-transport protein, characterized by high conservation during evolution. The volume offers the reader an updated, state-of-the-art summary of a field that is enjoying a true renaissance. Covering the topic from several viewpoints, the volume includes protein chemistry (amino acid sequence, secondary, tertiary and quaternary structures, thermodynamics of oxygen-binding features), molecular biology (globin gene structure, sequence, organization, expression and regulation) and evolution. In this representation of effective multidisciplinary and multina­ tional collaborative efforts, reference is available to a wide range of disciplines and biological systems. The tools of the investigators comprise advanced and powerful methodologies developed in recent years, e. g.

Molecular aspects of temperature adaptation; Adaptations for oxygen transport: lessons from fish hemoglobins; Recent evolution of the hemoglobinless condition of the Antarctic icefishes; Oxygen-transport system and mode of life in Antarctic fish; Functional properties of the cathodic hemoglobin component from two species of Anguilliformes; Oxygen transport in diving vertebrates; Oxygen transport and diving behaviour: the hemoglobin from dolphin Tursiops truncatus; Molecular modelling analysis of the hemoglobins of the Antarctic bird Catharacta maccormicki. The hypothesis of a second phosphate binding site.

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