1887

Abstract

SUMMARY:

All strains of and tested, were found to contain a blue protein; this has been named ‘Azurin’. It has been extracted from the cells of all three species and it has also been isolated from culture supernatant fluids of . The azurin was purified by chromatography on ion-exchange cellulose derivatives and obtained in physically pure form; the materials from each species were identical. In one strain of azurin comprised 0·1% of the bacterial dry weight. Azurin is a water-soluble autoxidizable protein of high oxidation-reduction potential (+395 mV.). It has an absorption maximum at 625 mμ in the oxidized form, with a millimolar extinction coefficient of 3·5 × 10. It contains 0·45% copper which can be completely removed by dialysis against cyanide. The molecular weight is 14,600 ( = 1·58 × 10, = 10·6 × 10). Azurin can be reduced by cysteine, glutathione and other reducing agents; the blue colour disappears on reduction. Azurin undergoes reduction in the presence of concentrated cell-free extracts of and succinate, and is reoxidized on aeration.

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/content/journal/micro/10.1099/00221287-30-1-105
1963-01-01
2022-01-23
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References

  1. Cohen S. M., Wheeler M. W. 1946; Pertussis vaccine prepared with phase-1 cultures grown in fluid medium. Amer. J. publ. Hlth 36:371
    [Google Scholar]
  2. Coval M. L., Horio T., Kamen M. D. 1961; The amino acid composition of some bacterial haem proteins. Biochim. Biophys. Acta 51:246
    [Google Scholar]
  3. Gibson J. 1961; Cytochrome pigments from the green photosynthetic bacterium, Chlorobium thiosulphatophilum. Biochem. J. 79:151
    [Google Scholar]
  4. Hammarsten E., Palmstierna H., Meyer E. 1959; Separation of acid polyelectrolytes and proteins in cellular extracts. J. biochem. microbiol. Tech. Eng. 1:273
    [Google Scholar]
  5. Horio Τ. 1958a; Terminal oxidation systems in bacteria. I. Purification of cytochromes from Pseudomonas aeruginosa. J. Biochem., Tokyo 45:195
    [Google Scholar]
  6. Horio T. 1958b; Terminal oxidation systems in bacteria. II. Some physical and physiological properties of purified cytochromes of Pseudomonas aeruginosa. J. Biochem., Tokyo 45:267
    [Google Scholar]
  7. Horio T., Sekuzu I., Higashi T., Okunuki K. 1961 Cytochrome oxidases of Pseudomonas aeruginosa and ox-heart muscle, and their related respiratory components. Haematin Enzymes302 Falk J. E., Lemberg R., Morton R. K. Oxford: Pergamon Press;
    [Google Scholar]
  8. Katoh S. 1960; A new copper protein from Chlorella ellipsoidea. Nature, Lond. 186:533
    [Google Scholar]
  9. Katoh S., Takamtya A. 1961; A new leaf copper protein ‘plastocyanin’, a natural Hill oxidant. Nature, Lond. 189:665
    [Google Scholar]
  10. Klotz I. M., Faller I. L., Urquart J. E. 1950; Spectra of copper complexes with some proteins, amino acids and related substances. J. phys. coll. Chem. 54:18
    [Google Scholar]
  11. Kohn J. 1959; A simple method for concentrating fluids containing protein. Nature, Lond. 183:1055
    [Google Scholar]
  12. Lysenko O. 1961; Pseudomonas—An attempt at a general classification. J. gen. Microbiol. 25:379
    [Google Scholar]
  13. Palmstierna H. 1960; A method for concentrating solutions of high molecular weight compounds. Biochem. Biophys. res. Comma. 2:53
    [Google Scholar]
  14. Postgate J. R. 1956; Cytochrome c3 and desulphoviridin ; pigments of the anaerobe Desulphovibrio desulphuricans. J. gen. Microbiol. 14:545
    [Google Scholar]
  15. Sutherland I. W., Wilkinson J. F. 1961; A new growth medium for virulent Bordetella pertussis. J. Path. Bact. 82:431
    [Google Scholar]
  16. Sutherland I. W., Wilkinson J. F. 1962; Azurin, a blue bacterial protein. Biochem. J. in the press
    [Google Scholar]
  17. Szturm S., Bourdon D. 1948; Bacterium akaligines fecalis et hemophilus bronchi-septicus; caractères morphologiques et biochimiques. Ann. Inst. Pasteur 75:65
    [Google Scholar]
  18. Verhoeven W., Takeda Y. 1956 The participation of cytochrome c in nitrate reduction. Inorganic Nitrogen Metabolism159 McElroy W. D., Glass B. Baltimore: The Johns Hopkins Press;
    [Google Scholar]
  19. Westerfeld W. W. 1961; Effect of metal-binding agents on metallo-proteins. Fed. Proc. 20:158
    [Google Scholar]
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