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A three-barrier model for the hemocyanin channel. [PDF]
Journal of General Physiology, 1981 Keyhole limpet hemocyanin forms ion-conducting channels in planar lipid bilayer membranes. Ionic current through the open hemocyanin channel presents the following characteristics: (a) it is carried mainly by cations; (b) it is a nonlinear function of ...
O Alvarez +5 more
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On the binding of copper by hemocyanin
Archives of Biochemistry and Biophysics, 1959Abstract One new sulfhydryl group can be determined by amperometric silver titration in several denaturing media, for each four atoms of copper removed from hemocyanin by anaerobic dialysis with neutral cyanide.
L C, THOMSON, M, HINES, H S, MASON
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Comparative Biochemistry and Physiology, 1965
Abstract 1. 1. The total sulfhydryl groups and the number of free SH groups of hemocyanins from different sources has been determined. Hemocyanins are well characterized by their content of “half cystine”, much more than by the content of any other amino acid. 2. 2.
A, Ghiretti-Magaldi, C, Nuzzolo
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Abstract 1. 1. The total sulfhydryl groups and the number of free SH groups of hemocyanins from different sources has been determined. Hemocyanins are well characterized by their content of “half cystine”, much more than by the content of any other amino acid. 2. 2.
A, Ghiretti-Magaldi, C, Nuzzolo
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Conversion of crustacean hemocyanin to catecholoxidase
Micron, 2004Crustacean hemocyanin as oxygen carrier and catecholoxidase as enzymes belong to the same protein family (type 3 copper proteins) sharing very similar active sites. Treatment with SDS of these hemocyanins results in an opening of the entrance to the active site for bulky phenolic compounds. This demonstrates, that almost all hemocyanin subunits possess
Elmar Jaenicke, Heinz Decker
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Hemocyanins in Spiders, XII. Dissociation and Reassociation ofEurypelmaHemocyanin
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1980The dissociation and reassembly of Eurypelma californicum hemocyanin was studied under various conditions of pH, ionic strength and protein, calcium and magnesium concentrations. The hemolymph concentrations of calcium and magnesium were determined to be ca. 4 and 0.9mM, respectively.
H, Decker +3 more
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Inorganica Chimica Acta, 1983
Abstract Our attempts to understand oxygen binding at the active site of the binuclear copper protein hemocyanin (Hc) [1] encompass two strategies. The first of those is the investigation of the structures and reaction chemistry of Cu(I) complexes ligated by nitrogenous donors since the deoxy form of hemocyanin is of this form.
Thomas N. Sorrel +3 more
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Abstract Our attempts to understand oxygen binding at the active site of the binuclear copper protein hemocyanin (Hc) [1] encompass two strategies. The first of those is the investigation of the structures and reaction chemistry of Cu(I) complexes ligated by nitrogenous donors since the deoxy form of hemocyanin is of this form.
Thomas N. Sorrel +3 more
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Journal of Chemical Education, 1976
The author contrasts hemocyanin against hemoglobin and discusses the occurrence of hemocyanin; oxygen and hemocyanin; the details of the oxygenation curves; Bohr effect and the respiration of squids and snails; and dissociation of association of hemocyanin.
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The author contrasts hemocyanin against hemoglobin and discusses the occurrence of hemocyanin; oxygen and hemocyanin; the details of the oxygenation curves; Bohr effect and the respiration of squids and snails; and dissociation of association of hemocyanin.
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Immunochemical properties of hemocyanin
Immunochemistry, 1964Abstract The immunochemical properties of the precipitation of anti-hemocyanin by associated and dissociated hemocyanin were found to be markedly different. The difference between the precipitation of associated and dissociated hemocyanin was observed with antibody to both the associated and dissociated hemocyanins.
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The FASEB Journal, 2017
Hemocyanin is the oxygen‐carrying protein in most mollusks and some arthropods. It is relevant to the study of natural selection as it evolved after hemoglobin. How do environmental factors affect the structure and the oxygen affinity of hemoglobin compared to the structure and the oxygen affinity of hemocyanin? The Ronald Reagan High
Molly Schuld +14 more
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Hemocyanin is the oxygen‐carrying protein in most mollusks and some arthropods. It is relevant to the study of natural selection as it evolved after hemoglobin. How do environmental factors affect the structure and the oxygen affinity of hemoglobin compared to the structure and the oxygen affinity of hemocyanin? The Ronald Reagan High
Molly Schuld +14 more
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Hemocyanins in Spiders, XVII. A Presumptive Active-Site Sequence of Arthropodan Hemocyanins
Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1982Peptides containing the sequence -His-His-Trp-His-Trp-His- have been isolated from the subunits e and a of tarantula (Eurypelma californicum) hemocyanin and III B of Limulus polyphemus hemocyanin. In view of the published spectroscopic and titration data on the copper-polypeptide complex and the strong quenching effect of oxygenation on hemocyanin ...
H J, Schneider +5 more
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