Beiträge zur enzymatischen Histochemie. XVI. Die Verdauung von Keratin durch die Larven der Kleidermotte (Tineola biselliella Humm.).

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Abstract
An extremelv active proteinse was detected by micro-methodsin the cells and juice of the middle intestine of tineolla biselliella, the common clothes moth. This proteinse had no effect on wool either at the optimal pH for casein (6.3 for 2hrs. at 40[degree]C) or at the pH of intestinal juice 96-10.2, which was not alkaline enough for cleavage keratin. Upon the addition of a reducing agent, lithium hydrogen sulfide ro thyglycolic acid, at pH 10, solution of the wool occured with cleavage of peptides. The intestinal juice of moths fed wool or crystine showed a pronounced positive reaction with nitroprusside unless the juice was exposed to the air; that of moths fed on a sulfur-poor diet gave a negative test. Reducing conditions, independent of a high content of sulfhydryl, in the middle intentine of the living moth were shown by feeding it an oxidation-reduction indicator. Trypsin kinase was found sensitive to sulfhydryl and inactive in the reducing medium required for decomposition of keratin.