Untersuchungen zur Reindarstellung des Magenkathepsins

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Abstract
Two different fractions of a hog gastric mucosa concentrate were separated by precipitation with 60 (NH4)S2O4 and electrophoresis. The cathepsin-containing fraction was enriched by multiple precipitation at pH 3.8; between pH 3.0 and 2.8 the pepsin/cathepsin ratio changes in favor of pepsin. Tiselius or paper strip electrophoresis results in 4 or 3 fractions; the faster contains most of the pepsin, the slower fractions, most of the cathepsin, the slowest fraction in paper strip electrophoresis has only slight enzymatic activity. Separation of the slower fractions in Tiselius electrophoresis results in a 4-fold increase of catheptic activity. Hog gastric mucosa contains 2 enzymatically active proteins, one of which seems to be pure pepsin, the other, with a high cathepsin activity, contains more or less pepsin activity. There is no evidence for a uniform gastric pro-teinase according to Freudenberg and Buchs (Schweiz. Med. Wochenschr. 79:249: 1940).
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