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Showing papers on "Tartrate-resistant acid phosphatase published in 1976"


Journal ArticleDOI
TL;DR: Low- and high-molecular-weight acid phosphatases were characterized by their elution volumes, specific inhibition and activity with two substrates and it is suggested that the distribution pattern found om rat tissues could be common to all eukaryotic cells.

68 citations


Journal ArticleDOI
TL;DR: Tissue-specific variations of enzyme activity occur: the specific activity of acid phosphatase in the frog femoral diaphysis is 437-, 2-, 3- and 1.2-fold greater than activities in the plasma, coracoid, femoral epiphysis, and femoral metaphysis, respectively.
Abstract: 1. 1. The basic characteristics of acid phosphatase in amphibian skeletal tissues and plasma are similar to those of mammals. 2. 2. The pH optimum of frog bone acid phosphatase is 4.2, while that of plasma is 4.4; at higher pH levels, enzyme activity rapidly declines. 3. 3. Normal kinetic patterns of acid phosphatase activity occur when substrate and enzyme concentrations, and time and temperature of incubation in enzyme assays are varied. 4. 4. Plasma acid phosphatase is thermolabile, losing 22% of its activity at room temperature (1 hr); half-inactivation occurs at 60°C. In contrast, bone acid phosphatase is thermostable, retaining its original activity from 25 to 80°C. 5. 5. Frog bone acid phosphatase is not particle-bound to heavy components of bone mineral or matrix, and is localized within the lysosomes of skeletal cells. 6. 6. Tissue-specific variations of enzyme activity occur: the specific activity of acid phosphatase in the frog femoral diaphysis is 437-, 2-, 3- and 1.2-fold greater than activities in the plasma, coracoid, femoral epiphysis, and femoral metaphysis, respectively.

4 citations