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13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2

  • Frank R. N. Gurd
  • Jon S. Morrow
  • Philip Keim
  • Ronald B. Visscher
  • Robert Marshall
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 48)

Abstract

This report deals with the prospects for 13C NMR in defining the interactions of CO2 and its hydrated derivatives with small molecules and various proteins. The importance of bicarbonate ion as a buffer component is well recognized. The insolubility of many bicarbonate and carbonate salts is a central fact around which most people interested in metal-protein interactions try to work. The most common strategy is to remove or at least to avoid adding bicarbonate while setting up a metal-peptide or metal-protein study. The availability of 13C-enriched CO2 and bicarbonate and of NMR spectrometers capable of studying the 13C signals makes it convenient to reexamine the roles of these important interacting species in certain metal-protein systems of unquestionable importance.

Keywords

Carbonic Anhydrase Human Hemoglobin Carboxyl Carbon Carbonate Salt White Leghorn Chicken 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1974

Authors and Affiliations

  • Frank R. N. Gurd
    • 1
  • Jon S. Morrow
    • 1
  • Philip Keim
    • 1
  • Ronald B. Visscher
    • 1
  • Robert Marshall
    • 1
  1. 1.Dept. of ChemistryIndiana Univ.BloomingtonUSA

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