Tissue fractionation studies. 7. Release of bound hydrolases by means of triton X-100

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Abstract
The bound forms of acid phosphatase, ribonuclease, deoxyribonuclease, cathepsin and B-glucuronidase were released quantitatively in preparations from rat liver exposed to 0.1% (v/v) Triton X-100. This detergent had no inhibitory effect on the enzymes. The above findings form the basis of a method whereby total activities of lysosomal enzymes can be assayed directly, without preliminary treatment of the liver preparations, simply by running the assays in the presence of 0.1% (v/v) Triton X-100. In mitochondrial preparations exposed to increasing concentrations of Triton X-100, the enzymes were released in a fairly abrupt fashion when the detergent concentration exceeded a certain critical level, which was about 0.035 % (v/v) for an amount of granules corresponding to 0.1 g of original tissue/ml. All 5 enzymes were liberated in a roughly parallel manner, but the scattering of the results was such that finer differences could not be excluded.