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Structure of panulirus interruptus hemocyanin and evolution of arthropod hemocyanin
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2020
Hemocyanin (Hc), a copper-containing extracellular multimeric protein, is the major protein component of hemolymph in different arachnid groups. Hc possesses 7 or 8 very well-characterized types of monomers with molecular weights ranging from 70 to 85 kDa, organized in hexamers or multiple of hexamers.
Cunningham, Monica Liliana +3 more
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Hemocyanin (Hc), a copper-containing extracellular multimeric protein, is the major protein component of hemolymph in different arachnid groups. Hc possesses 7 or 8 very well-characterized types of monomers with molecular weights ranging from 70 to 85 kDa, organized in hexamers or multiple of hexamers.
Cunningham, Monica Liliana +3 more
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2020
Instead of the red blood of vertebrates, most molluscs have blue hemolymph containing hemocyanin, a type-3 copper-containing protein. The hemoglobin of vertebrate blood is replaced in most molluscs with hemocyanin, which plays the role of an oxygen transporter.
Sanae, Kato +2 more
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Instead of the red blood of vertebrates, most molluscs have blue hemolymph containing hemocyanin, a type-3 copper-containing protein. The hemoglobin of vertebrate blood is replaced in most molluscs with hemocyanin, which plays the role of an oxygen transporter.
Sanae, Kato +2 more
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Bivalve hemocyanins—a comparison with other molluscan hemocyanins
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19881. The hemocyanins of the protobranch bivalves Yoldia thraciaeformis, Yoldia limatula and Acila castrensis have absorption spectra similar to other hemocyanins. 2. Hemocyanins from all three bivalves appear as six-tiered cylinders in the electron microscope (30-32 nm in diameter by 34-38 nm in height). Yoldia thraciaeformis and A.
N B, Terwilliger +3 more
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The Structure of Arthropod Hemocyanins
Science, 1985Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity.
Linzen, B. +16 more
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The incidence of hemocyanin-binding cells in hemocyanin-tolerant rats
Cellular Immunology, 1972Abstract The incidence of lymphoid cells which react in vitro with 125 I-labeled hemocyanin ( Jasus lalandii ) has been investigated using cells from normal rats and rats made tolerant to HCY by a neonatal course of injections. The absence of humoral or cellular responses to HCY in the tolerant rats was established by their failure to: 1) produce ...
M G, Cooper, G L, Ada, R E, Langman
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Multifunctional Roles of Hemocyanins
2020The copper-containing hemocyanins are proteins responsible for the binding, transportation and storage of dioxygen within the blood (hemolymph) of many invertebrates. Several additional functions have been attributed to both arthropod and molluscan hemocyanins, including (but not limited to) enzymatic activity (namely phenoloxidase), hormone transport,
Coates, Christopher J. +1 more
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Immunogenicity of Hemocyanins and their Subunits
The Journal of Immunology, 1969Abstract The primary, secondary and hyperimmune responses of rabbits to hemocyanin and hemocyanin subunits from three molluscan and three arthropod species were measured. The amount of antibody formed by hyperimmune animals was independent of molecular size when closely related molecular species were used.
A A, Amkraut, A, Malley, D, Begley
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