Literature DB >> 6477505

Removal of copper from Octopus vulgaris haemocyanin. Preparation of the half-apo and apo derivatives.

M Beltramini, F Ricchelli, A Piazzesi, A Barel, B Salvato.   

Abstract

The two copper ions bound in the active site of Octopus vulgaris haemocyanin can be removed by cyanide. The two metal ions react with the ligand sequentially. In this paper the preparation of Octopus half-apo-haemocyanin, containing at the active site a single copper ion, is described. Moreover, the conditions to obtain Octopus apo-haemocyanin, containing less than 3% of copper still bound, are given.

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Year:  1984        PMID: 6477505      PMCID: PMC1144124          DOI: 10.1042/bj2210911

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  7 in total

1.  Electron addition to the active site of Cancer magister haemocyanins. An ESR study of cu(II) centres after gamma-radiolysis.

Authors:  M C Symons; R L Petersen
Journal:  Biochim Biophys Acta       Date:  1978-08-21

2.  Acid-base titration of hemocyanin from Octopus vulgaris Lam.

Authors:  B Salvato; A Ghiretti-Magaldi; F Ghiretti
Journal:  Biochemistry       Date:  1974-11-05       Impact factor: 3.162

3.  Isotopic copper exchange in Pila haemocyanin with three radioactive cuprous complexes.

Authors:  J A Cox; F G Elliott
Journal:  Biochim Biophys Acta       Date:  1974-12-18

4.  Fluorescence properties of hemocyanin from Levantina hierosolima.

Authors:  N Shaklai; E Daniel
Journal:  Biochemistry       Date:  1970-02-03       Impact factor: 3.162

5.  Conformational changes of Carcinus maenas haemocyanin induced by urea.

Authors:  F Ricchelli; B Salvato; B Filippi; G Jori
Journal:  Arch Biochem Biophys       Date:  1980-06       Impact factor: 4.013

Review 6.  NEUTRAL SALTS: THE GENERALITY OF THEIR EFFECTS ON THE STABILITY OF MACROMOLECULAR CONFORMATIONS.

Authors:  P H VONHIPPEL; K Y WONG
Journal:  Science       Date:  1964-08-07       Impact factor: 47.728

7.  Hemocyanin of Octopus vulgaris. The molecular weight of the minimal functional subunit in 3 M urea.

Authors:  B Salvato; A Ghiretti-Magaldi; F Ghiretti
Journal:  Biochemistry       Date:  1979-06-26       Impact factor: 3.162

  7 in total

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