Invertebrate Oxygen Carriers

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53,49 

ISBN: 3540169431
ISBN 13: 9783540169437
Herausgeber: Bernt Linzen
Verlag: Springer Verlag GmbH
Umfang: xiv, 521 S., 252 s/w Illustr., 521 p. 252 illus.
Erscheinungsdatum: 01.10.1986
Auflage: 1/1986
Produktform: Kartoniert
Einband: Kartoniert
Artikelnummer: 5450301 Kategorie:

Beschreibung

The international conference on "Invertebrate Oxygen Carriers" took place from July 29th to August 1st, 1985, at Tutzing, in a pleasant setting on Lake Starn­ berg. It was the 8th in a series which started in 1966 with a meeting in Naples on the "Physiology and Biochemistry of Haemocyanins" organized by F. Ghiretti. The list of contributors and participants of the Naples meeting reports thirty names among which we find that of A. C. Redfield, a pioneer of this field. In Tutzing over 100 scientists came together to discuss their research on all types of oxygen transporting proteins. Clearly the invertebrate hemoglobins have received increasing attention, and a more unified view of their complex quaternary structure is emerging. Their sequences are becoming unravelled and their functions more rationally understood. Hemerythrins have been covered, and their mechanism of binding oxygen explained lucidly. In the hemocyanin field there were exiting new results at every structural level - the X-ray structure of Panulirus hemocyanin, a wealth of sequence data for both arthropodan and molluscan types of hemocyanin, the molecular dimension of native hemocyanins provided by cryo-electron microscopy. New insights into the evolution of copper proteins have been obtained. There are new approaches to explain allosteric interaction in such complicated systems. The scope of investigations reaches from molecular genetics to organismic physiology. The conference received major support from the Deutsche Forschungsgemeinschaft and from the Bayerisches Staatsministerium fUr Unterricht und Kultus.

Autorenporträt

InhaltsangabeOpening Session.- Homage to René Lontie.- Hemerythrins.- Structure, function and oxidation levels of hemerythrin.- Structure and Function of Invertebrate Hemoglobins.- The dissociation of the extracellular hemoglobin of Lumbricus terrestris: A model of its subunit structure.- Subunit structure of earthworm erythrocruorin.- Characterization of trimeric hemoglobin component from the earthworm, Lumbricus terrestris.- The structure of the extracellular hemoglobin of annelids.- Ophelia bicornis erythrocruorin. Some peculiar features.- Structure of annelid hemoglobins - small angle X-ray studies.- Structural analogies in annelid erythrocruorins.- Role of SH-groups and S-S bridges in the main subunit (1/12 molecule) of Spirographis spallanzanii chlorocruorin.- Subunit structure and amino acid sequence of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.- A preliminary study of the hemoglobin of Arenicola marina.- Oxygen equilibria of whole molecules, isolated subunits and the subunit trimer of hemoglobin from Lumbricus terrestris.- The amino acid sequence of a structural unit isolated from the high molecular weight globin chains of Artemia sp.- Quaternary structure and modulation of function in earthworm erythrocruorin.- Calcium dependent allosteric modulation and assembly of the giant hemoglobin from the earthworm, Eisenia foetida.- Quaternary structure of erythrocruorin from the aquatic snail Helisoma trivolvis.- Immunochemical properties of molluscan hemoglobins.- Studies of the heme environment in molluscan hemoglobins by EPR.- The cooperative dimeric hemoglobin from the mollusc Scapharca inaequivalvis: structural and functional characterization.- The low resolution structures of the cooperative hemoglobins from the blood clam Scapharca inaequivalvis.- Structure and function of the dimeric and tetrameric hemoglobins from the bivalve mollusc, Anadara broughtonii.- Cosolvent effects on hemoproteins' oxygen uptake and equilibria.- Hemoglobin from the parasitic barnacle, Briarosaccus callosus.- Sulfide-binding by an extracellular hemoglobin.- Structure of Arthropodan Hemocyanins.- Three-dimensional structure of haemocyanins from the spiny lobster Panulirus interruptus, at 3.2 Å resolution.- Primary structure of the a chain of Panulirus interruptus hemocyanin.- Subunits a, b and c of Panulirus interruptus hemocyanin and evolution of arthropod hemocyanins.- Primary structure of subunit b of Panulirus interruptus hemocyanin.- Amino acid sequence studies on the c chain of Panulirus interruptus hemocyanin.- Partial amino acid sequence of crayfish (Astacus leptodactylus) hemocyanin.- Hemocyanin of the spider Eurypelma californicum: amino acid sequence of subunit a and of the smaller CB-peptides of subunits b and c.- Mapping of antigenic determinants in Androctonus australis hemocyanin: preliminary results.- Circular dichroism spectra of native 37 S hemocyanin from the spider Eurypelma californicum and its subunits.- Subunit heterogeneity and aggregate formation in Cherax destructor and Jasus sp. hemocyanins.- On the role of individual subunits in the quaternary structure of crustacean hemocyanins.- STEM and cryo-TEM of Limulus and Kelletia hemocyanin.- Subunit Structure of Molluscan Hemocyanins.- Presence of only seven functional units in the polypeptide chain of the haemocyanin of the cephalopod Octopus vulgaris.- Immuno-EM of Sepia officinalis hemocyanin.- Preliminary results on the structure of Octopus dofleini hemocyanin.- Functional and structural properties of the 50,000 D subunit of Octopus vulgaris hemocyanin.- Immunochemical relationships and subunit composition of selected molluscan hemocyanins.- Kinetics and equilibria of Octopus hemocyanin association.- Subunit structure of hemocyanin from the gastropod Levantina hierosolima.- Evolution of Hemocyanins.- Partial primary structure of the Helix pomatia ?c-hemocyanin functional unit d.- Amino acid sequence of the C-terminal domain of octopus (Paroctopus

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