Results 141 to 150 of about 1,731 (177)
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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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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 ...
Agnes Henschen, Bernt Linzen
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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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Dissociation of Eriphia hemocyanin
Archives of Biochemistry and Biophysics, 1967Abstract Some aspects of the pH-dependent dissociation of a crustacean ( Eriphia spinifrons ) hemocyanin have been studied. We found that the largest molecules (~24 Svedbergs, molecular weight ~9.5 × 10 5 ) dissociate into two identical subunits (~16 Svedvergs, molecular weight ~4.5 × 10 5 ) which in turn dissociate into a not well-defined number of
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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2004
The carbohydrate content and composition of hemocyanins (Hcs) of three prosobranchs (gastropods), Rapana thomasiana, Megathura crenulata and Haliotis tuberculata, were compared. The analyses were performed by gas-liquid chromatography after methanolysis, re-N-acetylation and trimethylsilylation. The two structural subunits of R. thomasiana Hc, RtH1 and
Krassimira, Idakieva +3 more
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The carbohydrate content and composition of hemocyanins (Hcs) of three prosobranchs (gastropods), Rapana thomasiana, Megathura crenulata and Haliotis tuberculata, were compared. The analyses were performed by gas-liquid chromatography after methanolysis, re-N-acetylation and trimethylsilylation. The two structural subunits of R. thomasiana Hc, RtH1 and
Krassimira, Idakieva +3 more
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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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Hemocyanin of the chiton Acanthopleura granulata
Biochemistry, 1986The subunit structure and solution conformation of the hemocyanin of the chiton Acanthopleura granulata were investigated by light-scattering, ultracentrifugation, viscosity, absorbance, and circular dichroism methods. The molecular weight, determined by light scattering at pH 7.4 in the presence of 0.05 M Mg2+ and 0.01 M Ca2+, was (4.2 +/- 0.3) X 10(6)
T T, Herskovits +2 more
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