Abstract
Plimmer anci Bayliss1 showed as early as in 1906 that the phosphorus of casein could be completely removed as inorganic phosphate by the action of 1 per cent sodium hydroxide at 37° C. in 24 hr. Acidification of the digest after the completion of dephosphorylation precipitated a substance resembling casein. Rimington2 analysed the dephosphorized casein for its nitrogen distribution and noticed little difference in composition from that of casein except in amide and arginine nitrogen. The low values obtained in these two cases were evidently due to the hydrolytic action of alkali on these compounds with the production of ammonia. Plimmer and Lawton3 found besides that by the action of N/4 alkali on casein there was formed in addition to casein a substance or mixture of substances resembling a primary proteose. The use of alkali as a dephosphorylating agent was considered to be undesirable for these reasons.
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References
Plimmer, R. H. A., and Bayliss, W. M., J. Physiol., 33, 439 (1906).
Rimington, C. D., Biochem. J., 21, 204 (1927).
Plimmer, R. H. A., and Lawton, J. H. T., Biochem. J., 33, 530 (1939).
Mecham, D. K., and Olcott, H. S., J. Amer. Chem. Soc., 71, 3670 (1949).
Perlmann, G. E., J. Gen. Physiol., 35, 711 (1952).
Sundararajan, T. A., and Sarma, P. S., Biochem. J., 56, 125 (1954).
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SUNDARARAJAN, T., SARMA, P. Preparation of Dephosphorized Casein by an Enzymic Method. Nature 173, 685 (1954). https://doi.org/10.1038/173685a0
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DOI: https://doi.org/10.1038/173685a0
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