Abstract
Quantitation of the binding of carbon dioxide to the α-amino group of the β-subunits of hemoglobin by 13C-nuclear magnetic resonance techniques has enhanced our understanding of the function of hemoglobin [3, 5]. We have further extended the investigation of the role of carbon dioxide binding to peptide hormones [10,12]. Such binding represents a nonenzymatic, reversible, post-translational modification. If an intact amino terminal determines the biological fate or activity of any particular peptide hormone, then the addition of CO2 could provide regulation for the endocrine system of which that peptide is a component. Possible mechanisms include a charge alteration, addition of bulk, or modification fo metal binding [6].
Supported by NIH Grants RO1 AM-21121, HL-05556 and GM-1046 and the Insurance Medical Scientist Scholarship Fund Sponsored by American United Life. This is the 112th paper in a series dealing with coordination complexes and catalytic properties of proteins and related substances
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© 1980 Springer-Verlag Berlin Heidelberg
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Gurd, R.S., England, R.D., Hayes, D.F., Wittebort, R.J., Rothgeb, T.M. (1980). Formation and Physiological Role of Carbamino Adducts of Angiotensin, Bradykinin, and S-Methylglucagon. In: Bauer, C., Gros, G., Bartels, H. (eds) Biophysics and Physiology of Carbon Dioxide. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67572-0_12
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DOI: https://doi.org/10.1007/978-3-642-67572-0_12
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