Literature DB >> 3066572

Recent aspects of the subunit organization and dissociation of hemocyanins.

T T Herskovits1.   

Abstract

1. The hemocyanins of the arthropod phylum are built of multiples of hexamers consisting of 1,2,4,6 and 8 of such basic assemblies. Their molecular weights range from about 0.45 x 10(6) to 3.9 x 10(6) daltons. The basic hexameric unit consists of bean-shaped monomers organized in the form of two layers of trimers placed on top of one another. The subunits are heterogeneous, in most cases consisting of four or more electrophoretically different polypeptide chains. 2. Molluscan hemocyanins have an entirely different structure and pattern of assembly from the arthropodan hemocyanins. The basic assembly of the molluscan hemocyanins are decamers organized in the form of right-handed cylinders approximately 300 A in diameter and 140-190 A in height. Different species have one, two and sometimes more than two such assemblies forming correspondingly longer cylindrical particles with molecular weights ranging from about 3.3 x 10(6) to 13 x 10(6) daltons. Cephalopod and chiton hemocyanins consist of single decameric particles, while gastropods have hemocyanins organized of di-decamers or higher assemblies. The subunits of these hemocyanins are elongated protein chains with seven or eight folded globular domains, each housing a binuclear copper center capable of binding and delivering oxygen. 3. The dissociation behavior of the arthropod hemocyanin hexamers and di-hexamers with the hydrophobic urea series of reagents suggest polar and ionic interactions as the main sources of stabilization of the hexamers and the hexamer to hexamer contacts within the di-hexamers. 4. Dissociation studies with the same urea probes with the molluscan hemocyanins, however, suggest a different pattern of stabilization. The stabilization of the decamer to decamer contacts within the gastropod di-decamers appear to be predominantly polar and ionic with relatively few hydrophobic interaction sites. The dimer contacts within the decamers and the monomer to monomer contacts within the dimers observed in the octopus and chiton hemocyanins appear to be predominantly hydrophobic in nature. 5. The urea and the pH dissociation profiles of the single decameric assemblies of some of the octopus and chiton hemocyanins investigated by light-scattering molecular weight methods, have been fitted using either a two-species, decamer to dimer and decamer to monomer scheme of subunit dissociation or a three-species, decamer to dimer to monomer scheme of dissociation.(ABSTRACT TRUNCATED AT 400 WORDS)

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Year:  1988        PMID: 3066572     DOI: 10.1016/0305-0491(88)90179-4

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  7 in total

1.  Conformational states of the Rapana thomasiana hemocyanin and its substructures studied by dynamic light scattering and time-resolved fluorescence spectroscopy.

Authors:  Dessislava Georgieva; Daniel Schwark; Peter Nikolov; Krassimira Idakieva; Katja Parvanova; Karsten Dierks; Nicolay Genov; Christian Betzel
Journal:  Biophys J       Date:  2004-11-08       Impact factor: 4.033

2.  Rapana thomasiana grosse (gastropoda) haemocyanin: spectroscopic studies of the structure in solution and the conformational stability of the native protein and its structural subunits.

Authors:  P Dolashka; N Genov; K Parvanova; W Voelter; M Geiger; S Stoeva
Journal:  Biochem J       Date:  1996-04-01       Impact factor: 3.857

3.  Characterization of the carbohydrate moieties of the functional unit RvH1-a of Rapana venosa haemocyanin using HPLC/electrospray ionization MS and glycosidase digestion.

Authors:  Pavlina Dolashka-Angelova; Alexander Beck; Alexandar Dolashki; Mariano Beltramini; Stefan Stevanovic; Benedetto Salvato; Wolfgang Voelter
Journal:  Biochem J       Date:  2003-08-15       Impact factor: 3.857

4.  Structure and Characterization of Eriphia verrucosa Hemocyanin.

Authors:  A Dolashki; M Radkova; E Todorovska; M Ivanov; S Stevanovic; L Molin; P Traldi; W Voelter; P Dolashka
Journal:  Mar Biotechnol (NY)       Date:  2015-08-11       Impact factor: 3.619

5.  Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthropod hemocyanin.

Authors:  J Markl; T Burmester; H Decker; A Savel-Niemann; J R Harris; M Süling; U Naumann; K Scheller
Journal:  J Comp Physiol B       Date:  1992       Impact factor: 2.200

6.  Quaternary structure heterogeneity of oligomeric proteins: a SAXS and SANS study of the dissociation products of Octopus vulgaris hemocyanin.

Authors:  Francesco Spinozzi; Paolo Mariani; Ivan Mičetić; Claudio Ferrero; Diego Pontoni; Mariano Beltramini
Journal:  PLoS One       Date:  2012-11-15       Impact factor: 3.240

7.  Proteomics Studies on the three Larval Stages of Development and Metamorphosis of Babylonia areolata.

Authors:  Minghui Shen; Guilan Di; Min Li; Jingqiang Fu; Qi Dai; Xiulian Miao; Miaoqin Huang; Weiwei You; Caihuan Ke
Journal:  Sci Rep       Date:  2018-04-19       Impact factor: 4.379

  7 in total

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