Abstract
IN recent years some investigators have searched for a fœtal type of myoglobin1–4. The results obtained by Jonxis and Wadman2 and Rossi-Fanelli and co-workers3 suggest that some differences exist between the myoglobins of the adult and fœtal cow, particularly as regards resistance against alkali, solubility and ultra-violet spectral absorption. By using paper electrophoretic techniques, Singer et al. 4 showed the probable existence of a fœtal type of this muscle pigment in human beings. However, a sharp characterization of these fœtal proteins has not yet been accomplished. In this communication we report some experiments concerning the paper electrophoretic behaviour and the amino-acid composition of the adult and fœtal myoglobin of the cow.
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References
Theorell, H., “Advances in Enzymology”, 7, 265 (1947).
Jonxis, J. H. P., and Wadman, S. K., Nature, 189, 884 (1952). Wadman, S. K., thesis, Groningen (1953).
Rossi-Fanelli, A., Cavallini, D., and de Marco, C., Arch. Biochem. Biophys., 50, 496 (1954).
Singer, K., Angelopoulos, B., and Ramot, B., Blood, 10, 987 (1955).
Boardman, N. K., and Adair, G. S. A., Nature, 177, 1078 (1956).
de Duve, C., Acta Chem. Scand., 2, 264 (1948).
Stein, W. H., and Moore, S. (personal communication).
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TIMMER, R., VAN DER HELM, H. & HUISMAN, T. Amino-Acid Composition of Adult and Fœtal Myoglobin of the Cow. Nature 180, 239–240 (1957). https://doi.org/10.1038/180239a0
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DOI: https://doi.org/10.1038/180239a0
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