Über pankreatische Lyo- und Desmo-lipasen. IV. Abhandlung: Zur Kenntnis zellgebundener Enzyme der Gewebe und Drüsen in der von R. Willstätter und M. Rohdewald begonnenen Untersuchungsreihe.

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Abstract
By extraction with 100% glycerin, only 0.1-3% of the total lipase (Lyolipase: L) could be extracted from the fresh pancreas or the acetone dried preparation. The remain-dor, bound to the protoplasm: D), could be converted by autolysis into a soluble form. Lipase estimations, mainly stalagmometric, with tributyrin as substrate, occasionally with methylbutyrate, were carried out, in every case after "equalizing activation" by albumin + Na oleate + CaCl2 for the purpose of removing the effect of accompanying substances. Extraction and activation conditions were investigated. L and D were activated differently by the compensatory activator, L up to 5000-9000%, D (used in the form of a suspension of the glycerin extracted tissue) to 100%. Different fractions of L were characterized by their behavior on activation. The differences underlying this behavior are explained as due to the change in the colloidal carrier. In a 29% glycerin extract the separation of a crystalline protein, which showed lipase activity, was observed occasionally.

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