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Functional properties of carboxypeptidase-digested hemoglobins.

Publication ,  Journal Article
Bonaventura, J; Bonaventura, C; Brunori, M; Giardina, B; Antonini, E; Bossa, F; Wyman, J
Published in: Journal of molecular biology
February 1974

Duke Scholars

Published In

Journal of molecular biology

DOI

EISSN

1089-8638

ISSN

0022-2836

Publication Date

February 1974

Volume

82

Issue

4

Start / End Page

499 / 511

Related Subject Headings

  • Tyrosine
  • Time Factors
  • Protein Conformation
  • Protein Binding
  • Photolysis
  • Phosphates
  • Oxyhemoglobins
  • Ligands
  • Hydrogen-Ion Concentration
  • Histidine
 

Citation

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Bonaventura, J., Bonaventura, C., Brunori, M., Giardina, B., Antonini, E., Bossa, F., & Wyman, J. (1974). Functional properties of carboxypeptidase-digested hemoglobins. Journal of Molecular Biology, 82(4), 499–511. https://doi.org/10.1016/0022-2836(74)90244-7
Bonaventura, J., C. Bonaventura, M. Brunori, B. Giardina, E. Antonini, F. Bossa, and J. Wyman. “Functional properties of carboxypeptidase-digested hemoglobins.Journal of Molecular Biology 82, no. 4 (February 1974): 499–511. https://doi.org/10.1016/0022-2836(74)90244-7.
Bonaventura J, Bonaventura C, Brunori M, Giardina B, Antonini E, Bossa F, et al. Functional properties of carboxypeptidase-digested hemoglobins. Journal of molecular biology. 1974 Feb;82(4):499–511.
Bonaventura, J., et al. “Functional properties of carboxypeptidase-digested hemoglobins.Journal of Molecular Biology, vol. 82, no. 4, Feb. 1974, pp. 499–511. Epmc, doi:10.1016/0022-2836(74)90244-7.
Bonaventura J, Bonaventura C, Brunori M, Giardina B, Antonini E, Bossa F, Wyman J. Functional properties of carboxypeptidase-digested hemoglobins. Journal of molecular biology. 1974 Feb;82(4):499–511.
Journal cover image

Published In

Journal of molecular biology

DOI

EISSN

1089-8638

ISSN

0022-2836

Publication Date

February 1974

Volume

82

Issue

4

Start / End Page

499 / 511

Related Subject Headings

  • Tyrosine
  • Time Factors
  • Protein Conformation
  • Protein Binding
  • Photolysis
  • Phosphates
  • Oxyhemoglobins
  • Ligands
  • Hydrogen-Ion Concentration
  • Histidine