Existence of Several Active Components in Crude Pepsin Preparations

Abstract

THE original solubility measurements on crystalline swine pepsin led to the conclusion that the crystals consisted of a single pure protein or several closely related proteins1. Since that time, it has become apparent in this and other laboratories2,5 that pepsins prepared from the various commercial products or from pepsinogen differ in solubility, specific proteolytic activity and stability. Solubility measurements have now been made on various partially purified pepsin preparations in order to determine the cause of these variations.

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References

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    The hæmoglobin method used in this work has been described by Anson, J. Gen. Physiol., 22, 79 (1938), and is a modification of the previously described method (Anson and Slirsky, J. Gen. Physiol., 16, 59; 1932). The modified method gives results which are 1015 per cent higher than the old method and not lower as reported by Anson. The specific activity of 0·35 now found for the A component therefore represents an activity of about 0.31 by the method previously used.

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DESREUX, V., HERRIOTT, R. Existence of Several Active Components in Crude Pepsin Preparations. Nature 144, 287–288 (1939). https://doi.org/10.1038/144287b0

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