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From the Division of Laboratories and Research, New York State Department of Health, Albany
Abstract
Previous experiments demonstrated that the neutralizing potency of antimeningococcus serum, as shown by the phenomenon of local skin reactivity, is associated with the water-insoluble globulin as are the agglutinative and precipitative activities (1). This fraction was effectively separated from immune horse sera which differed in water-insoluble globulin content, when the sera were dialyzed, diluted with distilled water, and acidified to the point of maximum precipitation. A preliminary report of the results of further purification of the active fraction is now presented.
Three methods were applied: precipitation of the inert protein by zinc or aluminum chloride, isoelectric fractionation, and fractional solution in dilute sodium chloride. The first two procedures with the exception of certain modifications were similar to those used by Felton (2, 3) in the purification of the potent fraction of antipneumococcus serum.
Precipitation of inert protein with zinc chloride was carried out as follows: The isoelectrically precipitated globulin was dissolved in 1 per cent sodium chloride and the reaction was adjusted to pH 7.6.
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