Alkaline phosphatase in serum and liver in patients with cholelithiasis.
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An equation is presented which makes it possible to estimate the exchange activity of glucose-6-phosphatase, as a percentage of the hydrolytic activity, for a given concentration of substrate and acceptor. The quantitative significance of the exchange-inhibition phenomenon is discussed.
Phosphate-repressible phosphatase synthesis occurs in the algae, Euglena gracilis. This phenomenon differs from the similar process known to occur in bacteria in that (i) the enzyme is an acid rather than an alkaline phosphatase, and (ii) enzyme activity nearly disappears after addition of phosphate to the culture.
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Pan, Yue-Liang (University of Michigan Medical School, Ann Arbor), and Harold J. Blumenthal. Correlation between acid phosphatase and coagulase production or phage type of Staphylococcus aureus. J. Bacteriol. 82:124-129. 1961.-A quantitative assay of acid phosphatase in 26 coagulase-negative and 73 coagulase-positive strains of Staphylococcus aureus was performed using an assay procedure modified to estimate extracellular, as well as the cellular, phosphatase. Some of the factors affecting the formation of acid phosphatase were studied. On the average, coagulase-negative strains produced 4.0 units and coagulase-positive strains 19.6 units although some negative strains produced more phosphatase than positive strains. More phosphatase was produced by strains of phage-group I than by strains of any other group.
Garen, A. (University of Pennsylvania, Philadelphia) and H. Echols. Properties of two regulating genes for alkaline phosphatase. J. Bacteriol. 83:297-300. 1962.-A constitutive mutation in one of the two regulating genes for alkaline phosphatase has two effects on the synthesis of the enzyme: repression of synthesis is blocked, and the cell's capacity to produce the enzyme is reduced. The behavior of this type of mutation has been studied in heterozygotes. The results suggest that the product of this regulating gene functions as an inducer as well as a repressor.
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The paper reports a study of the distribution of phosphatases in the femora of three specimens of Humboldt's woolly monkey (Lagothrix humboldti) suffering from chronic hyperparathyroidism. Bone structure ranged from the apparently normal to extreme osteitis fibrosa. Most marked changes were found in the distribution of alkaline phosphatase, which reached at least 10 times the normal levels in the bone of the second monkey in the series, dropping to levels still well above normal in that of the most severely affected animal. Very high concentrations were found in the deeper layers of hypertrophied growth cartilage and in the osteoblasts lining poorly calcified trabeculae, and high concentrations in the fibre bone of the third animal. Lack of mineralization and the development of osteitis fibrosa are thus associated with a marked increase in alkaline phosphatase activity. Osteoclasts reacted strongly for acid phosphatase but were negative for alkaline phosphatase. Acid phosphatase levels were comparatively high in fibre bone, but overall levels ranged from 1/20 to less than 1/100 those of alkaline phosphatase. Some slow staining for acid phosphatase probably represents residual activity at acid pH of the markedly increased alkaline phosphatase. There may be some association between a failure of mineralization and the presence of acid phosphatase in osteoclasts and osteoid. The aetiology of the monkeys' condition is discussed. It seems likely that the parathyroid hypertrophy and rachitic changes were caused by low blood calcium dependent on a low calcium diet and lack of vitamin D, in which the requirements of New World monkeys are reputedly high.
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