Titlebook: Invertebrate Oxygen Carriers; Bernt Linzen Conference proceedings 1986 Springer-Verlag Berlin Heidelberg 1986 Calcium.Mollusca.Peptide.X-r

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Structure, Function and Oxidation Levels of Hemerythrinemerythrins pose interesting evolutionary, physiological, and chemical contrasts to the more widespread hemoglobins. Perhaps the most intriguing question to a chemist is: how does nature adapt a non-heme iron site to reversibly bind molecular oxygen?

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Structural Analogies in Annelid Erythrocruorinsf the electron-micrographs of these proteins, some debated experimental data divide the scientific community, e.g. the Mr of the whole molecule (ranging from 2,500 to 4,1000 kDa) and, in consequence, the Mr of the 1/12 molecules, the Mr and number of the smallest covalently bound subunits and the Mr

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Subunit Structure and Amino Acid Sequence of the Extracellular Hemoglobin from the Polychaete ,t (chain I) and a disulfide-bonded trimer of chains IIA, IIB, and IIC(1–4). Each chain is linked to one heme(1,5). As the first step for construction of a model of the molecular assembly of a giant multisubunit hemoglobin, we determined the amino acid sequences of all the constituent polypeptide cha

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Oxygen Equilibria of Whole Molecules, Isolated Subunits and the Subunit Trimer of Hemoglobin from ,Three of the chains form a disulfide linked trimer. Oxygen equilibria of the intact molecule are consistent with previous reports (1, 2) but prior incubation at low or high pH does not result in the irreversible changes reported for the same or similar hemoglobins (3, 4). Oxygen equilibria of the is