CHEMICAL PROPERTIES OF PORCINE LEUKOCYTE LYSOSOMAL HYDROLASES

Specific activities, pH optima and activation energies were determined for some of the acid hydrolases found in various sedimentation fractions of sonicated porcine leukocytes and for hydrolases solubilized by n-butyl alcohol extractions of leukocytes. Lysosomal enzyme latency was demonstrated for these hydrolases by suspending sediments from differential contrifugation in 0.0125–0.25M sucrose solutions and releasing the enzymes. Activation energies of some hydrolases especially cathepsin D and β-glucuronidase were low suggesting that these acid hydrolases could function efficiently during low temperature aging of meat. pH optima are compared to those of similar enzymes from other sources.

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