CHICK allantoic fluid interferon has been purified to various extents by several groups of workers. Among those who prepared interferon of high specific activity, Lampson et al.1 achieved a purification factor of 1830 after treatment with perchloric acid, concentration with zinc acetate and two fractionations on ‘CM-cellulose’. Such material still contained an inactive protein component that was only removed by electrophoresis on ‘Pevikon’. The final material had been purified 4,500 times. Fantes et al.2 purified interferon several thousand times by adsorption on ‘Doucil’, elution with KSCN, precipitation of impurities in the presence of KSCN at pH 3.5, precipitation of interferon with methanol at pH. 7.5 and chromatography on DEAE cellulose at pH. 7.5. Merigan3 purified crude interferon with perchloric acid and zinc acetate by the method of Lampson et al.1, achieving a 15-fold purification. Such material, after one chromatographic fractionation on ‘CM-Sephadex’, using a pH gradient instead of Lampson's stepwise process for eluting the active ingredient, was claimed to be purer than Lampson's material, though no evidence of electrophoretie homogeneity was presented.
Lampson, J. P., Tytell, A. A., Nemes, M. M., and Hilleman, M. R., Proc. Soc. Exp. Biol. and Med., 112, 408 (1963).
Fantes, K. H., O'Neill, C. F., and Mason, P. J., Biochem. J., 91, 20P (1964).
Merigan, T. C., Science, 145, 811 (1964) (and personal communication).
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Biol. Chem., 193, 265 (1951).
Baron, S., Barban, S., and Buckler, C. E., Science, 145, 814 (1964).
Olin Mathieson Chemical Corp., U.S.P. 195,428; German patent 1,179,332.
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Suppression of the accumulation of steroid-inducible glutamine synthetase mRNA on embryonic chick retinal polysomes by interferon preparation
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