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PROCEEDINGS OF THE PHYSIOLOGICAL SOCIETY: February 22, 1908

It has long been known that the protamines in alkaline (ammoniacal) solution possess the property of precipitating many other proteins, but the precise qualitative and quantitative relations of the reaction have not been thoroughly worked out. Last summer under Professor A. Kossel's direction I examined from this point of view a considerable number of proteins and related bodies'. It was found that while protamine combined in definite proportions with all native proteins (including such widely different substances as crystallised egg-albuimin, edestin, and gelatine), and also with primary proteoses (whether of the protoor heterogroup), it failed to react with any of the remoter products of hydrolysis, whether secondary proteoses, peptones, or polypeptides. I have subsequently found this distinctiorn capable of some useful practical applications, as for example in following qualitatively the course of a peptic digestion, or in testing the freedom from primary proteoses of a preparation of the secondary ones. For these and similar purposes a 1 per cent. ammoniacal solution of clupeine sulphate supplies a convenient and delicate test. The reaction is an extremely sharp one. Solutions of Witte's peptone so dilute as to give a hardly appreciable biuret reaction, and no reaction whatever with nitric acid or copper acetate, yet show with the protamine test an almost immediate