Titlebook: Respiratory Pigments in Animals; Relation Structure-F Jean Lamy (Scientific Editor),Jean-Paul Truchot (S Conference proceedings 1985 Spring

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logy and Biochemistry I organized at LI~e (Belgium) in August 1984 under the auspices of the Section of Comparative of the International Union of Biological Sciences. In a Physiology and Biochemistry general foreword to these different volumes, it seems to me appropriate to consider briefly what may

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The Structure of Erythrocruorins and Chlorocruorins, the Invertebrate Extracellular Hemoglobins,unctional globin genes or to defects in the mechanism regulating their expression. In the absence of information concerning the structure and expression of invertebrate globin genes, I would like to focus on the identification of common structural themes among these molecules. All the extracellular

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Functions and Functioning of Crustacean Hemocyanin,as poorly known at the time of Wolverkamp and Waterman’s (1960) chapter on respiration in Waterman’s “Physiology of Crustacea” and today, 25 years later, although our data base is much expanded our knowledge is still rudimentary compared with that for say mammalian Hb. In functional terms we have ab

Anticoagulants

Primary Structure of Arthropod Hemocyanins,f the blood between one and two orders of magnitude and thus provide the basis for continuous high activity. There are three types of such carriers which bind oxygen by different principles: (i) The hemoglobins, in which . Fe(II) is bound by a protoporphyrin plus one histidine residue of the globin.

DEI

Quaternary Structure of Arthropod Hemocyanins, composed of six kidney-shaped (70–75 kDa) subunits. This basic structural unit, called hexamer or (1×6)-mer, is a constituent of both crustacean and cheliceratan hemocyanins. Crustáceas contain (1×6)- meric hemocyanins in the spiny lobster . or in the shrimp ., (2×6)-mers in most species, and tetra

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Cephalopod Hemocyanins: Structure and Function,own to have hemocyanin; instead, a number use hemoglobin for oxygen transport. All known molluscan hemocyanins share some common features of molecular architecture. The individual polypeptide chains are large (300,000–400,000 daltons) multi-domain structures. Each domain, of which there may be 6–8,

Atheroma

Molecular and Cellular Adaptations of Fish Hemoglobin-Oxygen Affinity to Environmental Changes,mical parameters of their environments. For example, fish that live in low oxygen environments have high oxygen affinities while those that live in high oxygen environments have lower oxygen affinities. Moreover, fish that live in environments where physical parameters periodically change, have the

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Evolution and Adaptation of Avian and Crocodilian Hemoglobins,bly arose directly from the primitive cotylosaurs during the Triassic period some 220 millions years ago. These thecodonts gave rise to crocodiles during the Jurassic period and birds during the Triassic about 150 millions years ago.