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  • 1
    Electronic Resource
    Electronic Resource
    Specific IgG activity of sera from Egyptian schistosomiasis patients to keyhole limpet hemocyanin (KLH) (1991)
    Springer
    Naturwissenschaften 78 (1991), S. 30-31 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01134040
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  • 2
    Electronic Resource
    Electronic Resource
    Hemocyanins in spiders (1980)
    Springer
    Journal of comparative physiology 140 (1980), S. 199-207 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. The hemocyanin of the lycosid spiderCupiennius salei was separated into its hexameric (16 S) and dodecameric (24 S) components, and analyzed quantitatively. The reassociation and topologic distribution of the subunits were studied. 2. There are two types of subunits. One is monomeric (5 S) and consists of 5 electrophoretically distinct bands which are, however, immunologically identical. The other is a disulphide bridged dimer (7 S) which yields 2 components upon electrophoresis or immunoelectrophoresis. The significance of this heterogeneity was not studied. The dimer is antigenically deficient with respect to the monomer. 3. Whereas the 16 S hemocyanin is composed of six monomers, 24 S hemocyanin contains 10 monomers and 1 dimer. 4. Alkaline dissociation of 24 S hemocyanin (dodecamer) into subunits passes through a heptameric state (18 S) which is composed of 5 monomers and the dimer. In the electron microscope, 16 S-like units with a seventh polypeptide attached can be distinguished. 5. Treatment of 24 S or 18 S hemocyanin with reducing agents to cleave the disulphide bridge leads to a second type of hexamer (16 S′) which is electrophoretically distinct from native hexamers (16 S), and composed of 5 monomers and one constituent polypeptide chain of the dimer. 6. Upon dialysis of a monomer/dimer mixture against neutral buffer containing 40 mM calcium, 16 S, 18 S and 24 S particles are formed. The three reconstituted hemocyanins exhibit subunit compositions identical to the native hemocyanins and the 18 S component obtained during dissociation. 7. The results suggest that the 24 S hemocyanin particle consists of two identical hexamers linked by the disulphide bridge of a dimeric subunit shared by both hexamers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690404
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  • 3
    Electronic Resource
    Electronic Resource
    Subunit-specific monoclonal antibodies to tarantula hemocyanin, and a common epitope shared with calliphorin (1989)
    Springer
    Journal of comparative physiology 159 (1989), S. 139-151 
    Details
    ISSN: 1432-136X
    Keywords: Calliphorin ; Hemocyanin ; Monoclonal antibodies ; Evolution ; Spiders
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Three murine hybridoma cell lines secreting IgG1 antibodies to 4×6 tarantula (Eurypelma californicum) hemocyanin were isolated, and the monoclonal antibodies Ec-7, Ec-8 and Ec-24 characterized by immunoblotting, immunoelectrophoresis and ELISA. WholeEurypelma hemocyanin, and the isolated subunitsa tog served as probes. For the subunits a novel, quick purification scheme on FPLC combined with immuno-affinity chromatography was established. Additionally, two cell lines secreting IgM antibodies were isolated. These antibodies showed irrelevant cross reactivities. Ec-7 strongly reacts with subunitd and weakly withb. Ec-8 and Ec-24 are specifically directed againstEurypelma subunitsa ande, respectively. The epitopes of Ec-7 and Ec-8 are sequence-dependent, whereas the Ec-24 epitope is conformation-dependent. Ec-8 and Ec-24 are specific forEurypelma hemocyanin. Ec-7 is not reactive to crustacean, centipede or gastropod hemocyanins, but binds to scorpion hemocyanin and to the immunological correlates of subunitsd andf in the hemocyanins of the spiderCupiennius salei and the xiphosuranLimulus polyphemus. In immunoblots with different polyclonal antisera,Eurypelma andAstacus hemocyanin cross-reacted with calliphorin, a larval serum protein from the blowflyCalliphora vicina. Calliphorin and chelicerate hemocyanins share the Ec-7 epitope. Sedimentation coefficients, pH stability regions, subunit size, and electron microscopical appearance of calliphorin are indiscernable from a typical 1×6 arthropod hemocyanin. This relationship is discussed in the context of hemocyanin evolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00691734
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  • 4
    Electronic Resource
    Electronic Resource
    The quaternary structure of four crustacean two-hexameric hemocyanins: immunocorrelation, stoichiometry, reassembly and topology of individual subunits (1988)
    Springer
    Journal of comparative physiology 158 (1988), S. 271-289 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Two-hexameric (2×6) hemocyanins from the brachyuran crabsCancer pagurus andCallinectes sapidus, the freshwater crayfishAstacus leptodactylus and the lobsterHomarus americanus were isolated and dissociated into native subunits. The subunits of each hemocyanin were analyzed by electrophoresis and immunology. Three immunologically distinct subunit types, which were termedα,β andγ, could be identified in each case. They were isolated preparatively, and interspecifically correlated. Subunitα is subdivided into several electrophoretically distinct isoforms which are immunologically closely related (Astacus) or identical (other species). InAstacus andCancer one of these isoforms was shown to dimerize and to act as inter-hexamer bridge. It represents a fourth subunit type termedα′. A fifth, ‘diffuse’ component, which in PAGE migrated at the position of a dimer, was identified in the crossed immunoelectrophoretic patterns as denatured hemocyanin. A common feature of the four hemocyanins is the presence of 4 copies ofβ and 8 copies ofα/γ within the 2×6 particles. Theα:γ ratio is 4:4 in the two Astacidea and 6:2 in the two Brachyura.α′ exists in 2 copies inAstacus andCancer which means that a single dimerα′-α′ is present in a two-hexamer. This leaves 2 monomericα copies inAstacus and 4 inCancer. Every subunit from the four species except ofAstacus α′-α′ was capable to form hexamers in reassembly experiments. If subunit combinations were tested, hetero-hexamers were formed preferentially. Two-hexamers were reconstituted only in the presence of all subunit types and the native subunit stoichiometry was required to obtain twohexamers in considerable yields. Factors limiting 2×6 reassembly are discussed. Authentic 2×6 molecules ofAstacus, Homarus andCancer hemocyanin were immunolabeled with subunit-specific antibody fragments (Fab) or IgG molecules, and the resulting immuno complexes were studied in the electron microscope. A topological model of the quaternary structure of decapod 2×6 hemocyanins is derived, showing the position of each copy of the four subunit types. In this model, the inter-hexamer bridgeα′-α′ is surrounded by twoβ and twoγ subunits forming the central core of the dodecamer. Two additionalβ and two additionalγ subunits form the periphery together with oneα subunit occupying the peripheral short edges of each hexameric half structure. The model is discussed with respect to the current literature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00695326
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  • 5
    Electronic Resource
    Electronic Resource
    Subunit heterogeneity in crustacean hemocyanins as deduced by two-dimensional immunoelectrophoresis (1981)
    Springer
    Journal of comparative physiology 141 (1981), S. 495-502 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. Multiple subunits of hemocyanins from 3 brachyuran crabs (Carcinus maenas, Cancer pagurus, Hyas araneus), a spiny lobster (Palinurus vulgaris), a freshwater crayfish (Astacus leptodactylus), and a lobster (Homarus americanus) were isolated by preparative polyacrylamide gel electrophoresis (PAGE), and compared by two-dimensional immunoelectrophoresis. 2. In the 24 S hemocyanin isolated from each of the 3 crabs, two of the four subunits separated are immunologically identical; the third subunit is antigenically deficient compared to the first two. The fourth chain is immunologically unrelated to the other three. 3. In the 16 S hemocyanin ofPalinurus two of the four subunits are immunologically identical; the third is closely related. The fourth chain is partially identical with the other three, but is antigenically deficient. 4. The 16 S hemocyanin ofAstacus is composed of two immunologically unrelated subunits. The 24 S hemocyanin of this species contains, in addition, a dimeric subunit which is partially identical with one of the former, but not related to the other. 5. In the 24 S hemocyanin fromHomarus, five subunits were separated; a group of 2, and a group of 3 subunits which are immunologically identical, but which are not related to each other. 6. At the level of quaternary structure, a common principle is suggested for crustacean hemocyanins: 24 S hemocyanins are composed of three types of subunits, while 16 S hemocyanins contain only two types.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01101472
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  • 6
    Electronic Resource
    Electronic Resource
    Electron microscopy of a double helical tubular filament in keyhole limpet (Megathura crenulata) hemolymph (1992)
    Springer
    Cell & tissue research 269 (1992), S. 411-420 
    Details
    ISSN: 1432-0878
    Keywords: Hemolymph ; Filaments ; Hemocyanin ; Hemocytes ; Megathura crenulata (Mollusca)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A ≈25 nm hollow double helical filament has been detected ultrastructurally in the cell-free supernatant from hemolymph of the keyhole limpet Megathura crenulata (Gastropoda: Prosobranchia: Fissurellidae). Subsequently, much higher concentrations of this material were found in the cell pellet from hemolymph. Both negative staining and thin sectioning have been performed in an attempt to obtain a preliminary structural characterization of this new filament. It is proposed that the filaments are released or secreted from blood hemocytes in response to bleeding, but it has not been possible to define absolutely an intracellular organelle containing this material. It is shown that the hollow filaments, which have fine fibrillar surface extensions, are readily distinguishable from collagen fibrils and from tubular (multi-decameric) keyhole limpet hemocyanin (KLH).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00353896
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  • 7
    Electronic Resource
    Electronic Resource
    Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthropod hemocyanin (1992)
    Springer
    Journal of comparative physiology 162 (1992), S. 665-680 
    Details
    ISSN: 1432-136X
    Keywords: Hemocyanin ; Arylphorin ; Larval serum proteins ; Evolution ; Arthropods
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Arylphorin was purified from larvae of the blowfly Calliphora vicina and studied in its oligomeric form and after dissociation at pH 9.6 into native subunits. In accordance with earlier literature, it was electrophoretically shown to be a 500 kDa hexamer (1×6) consisting of 78 kDa polypeptides (= subunits). Electron micrographs of negatively stained hexamers show a characteristic curvilinear, equilateral triangle of 12 nm in diameter (top view) and a rectangle measuring 10×12 nm (side view). Alternatively, particles in the top view orientation exhibit a roughly circular shape 12 nm in diameter. Crossed immunoelectrophoresis revealed the presence of a major subunit type; the nature of a very minor and a third immunologically separated component remains unclear. A novel 2×6 arylphorin particle was detected and isolated. It comprises less than 10% of the total arylphorin material and shows a long, narrow interhexamer bridge in the electron microscope. An arylphorin dissociation intermediate identified as a trimer (1/2×6) was isolated; its possible quaternary structure is discussed on the basis of electron micrographs. The epitope of monoclonal antibody Ec-7 directed against tarantula (Eurypelma californicum) hemocyanin subunit d and also reactive to Calliphora arylphorin was traced to a highly conserved peptide of 27 amino acids localized in the center of the protein. The primary structure of Calliphora arylphorin as published in our preceding paper (Naumann and Scheller 1991) is compared in detail to the sequences of spider and spiny lobster hemocyanin. This revealed a basic framework of 103 strictly conserved amino acids. Isofunctional exchanges are proposed for another 76 positions. On the basis of these similarities, and the published three-dimensional model of spiny lobster hemocyanin, a detailed model of the quaternary structure of Calliphora arylphorin is presented. A second larval storage protein previously termed protein II was purified from Calliphora hemolymph. It was demonstrated to be a 500 kDa hexamer of 83 kDa subunits. In the electron microscope it shows a cubic view 9 nm in length with a large central hole and a rectangular view (9×10 nm) with a large central cavity. A morphologically very similar hemolymph protein was detected in Drosophila melanogaster larvae. From its structural appearance it is uncertain whether protein II belongs to the hemocyanin superfamily or not.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301616
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  • 8
    Electronic Resource
    Electronic Resource
    Blaues Blut - Struktur, Funktion und Evolution der Hämocyanine (1996)
    Weinheim : Wiley-Blackwell
    Chemie in unserer Zeit 30 (1996), S. 6-18 
    Details
    ISSN: 0009-2851
    Keywords: Chemistry ; Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ciuz.19960300103
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  • 9
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    Identification of keratins and analysis of their expression in carp and goldfish: comparison with the zebrafish and trout keratin catalog (2005)
    Springer
    Details
    Publication Date: 2005-07-30
    Print ISSN: 0302-766X
    Electronic ISSN: 1432-0878
    Topics: Biology , Medicine
    Published by Springer
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  • 10
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    Rhogocytes (pore cells) as the site of hemocyanin biosynthesis in the marine gastropod Haliotis tuberculata (2001)
    Springer
    Details
    Publication Date: 2001-05-28
    Print ISSN: 0302-766X
    Electronic ISSN: 1432-0878
    Topics: Biology , Medicine
    Published by Springer
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