Monolayers of proteolytic enzymes and proteins

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Abstract
III. It was possible to extract from pancreatin a fatty acid-protein complex which simulated the action of enzymes on monolayers of protein and fats at an air-liquid interface. This behavior explained the activity, toward surface films, of pancreatin preparations which were inactive in bulk. Specific proteolytic ferments did not contain this complex and consequently behaved towards protein mono-layers as they did in bulk.[long dash]IV. A study of 2-component unimolecular films by the methods of surface potentials and surface pressures (the components being long-chain alcohols, acids, glycerides, sphingosine and psychosine), showed that, on compression of a mixed film, either one component displaced the other from the surface, or both components remained as a stable mixed film. In the latter case there was evidence of the existence of a complex between the 2 components which did not involve measurable dipole interaction. In such cases the same mixed film was obtained by injection of the one component into the soln. beneath a film of the other component. This process, termed penetration, was followed, in certain cases, by complete displacement of the original film.

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