A NEW DIPHTHERIA ANTITOXIN
The preparation of a new highly purified diphtheria antitoxin of allegedly superior therapeutic properties and almost complete freedom from allergic toxicity has been recently announced by Pope and his colleagues1 of the Wellcome Laboratories, England. The technic by which this purification was accomplished involved a by-product of a study of heat denaturation of serum proteins. An antidiphtheritic serum containing 7,000 antitoxin units per gram of dissolved protein was changed to a serum fraction containing 27,000 antitoxin units per gram of protein. The result was ascribed to the action of a fibrinolytic enzyme in the serum fraction. A method of large scale purification of diphtheria antitoxin based on this fractional enzymic action has been developed; animal tests of this refined antitoxin indicate that it is more rapidly and completely absorbed from subcutaneous tissues than native antitoxin. It is also retained longer in the bodies of injected
Current Comment. JAMA. 1939;113(4):326. doi:10.1001/jama.1939.02800290052013
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