Studies on diffusing factors

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Abstract
A method of assaying hyaluronidase was described, which depended upon the destruction by the enzyme of the power of a substrate-protein complex to form a typical "mucin clot" on the addition of acetic acid. The limits of accuracy of the test and the influence of various environmental faptors on the reaction were studied. The relation between this change in the precipitability of the substrate and the viscosity-reducing activity of the enzyme was examined. The destruction of the clotting power of the substrate was an early stage in its degradation, which could be detected before any appreciable fall in viscosity occurred. Inhibition of the mucin clot prevention reaction by sera prepared against enzymes from various sources was studied. Sera which inhibited the diffusing and viscosity-reducing activity of these enzymes also inhibited the main-clot prevention reaction. Sera prepared against enzymes obtained from Cl. welchii and Vibrion septique were species[long dash]but not type-specific. Those obtained against streptococcal enzymes were group[long dash]but not type-specific. A serum prepared against diffusing factor from bulls'' testis inhibited this enzyme, but did not inhibit a testicular enzyme from the mouse, or any of the bacterial enzymes. Both the apparent pH optimum of viscosity-reducing activity, and the titre of the enzyme, were markedly affected by the conc. and nature of salts in the system. The bearing of these observations on the pH optima previously reported for the group of enzymes and on the correlation between different methods of assaying enzymic activity was discussed. Nine enzymes from various sources were examined for diffusing activity in the skin, by viscosimetry and by the mucin clot prevention test. The correlation that obtained between the 3 different methods of testing was described and the conclusion was drawn that all 3 tests measured the activity of the same agent.

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