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KMID : 0903519770200020175
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1977 Volume.20 No. 2 p.175 ~ p.181
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Chemical Properties of Porcine Leukocyte Lysosomal Hydrolases
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Abstract
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Lysosomal enzyme latency was demonstrated for hydrolases from porcine leukocyte by suspending sediment sfrom differential centrifugation in 0.125 to 0.250 M sucrose. Specific activities pH optima and activation energies were determined for hydrolases distributed in various sedimentation fractions and for enzymes solubilized by n-butyl alcohol extraction. Specific activities of the hydrolases revealed the heterogeneity of the lysosomal fractions relative to enzyme content. pH optima identified the enzyme as acid hydrolases with optima for cathepsin D and aryl sulfatase also at pH 6.8. Activation energies of some hydrolases were low revealing that these enzymes could function efficiently during low temperature aging of meat.
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