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
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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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