THE EFFECT OF THYROPROTEIN AND PROPYLTHIOURACIL FEED SUPPLEMENTATION ON CALCIUM LEVELS AND ALKALINE PHOSPHATASE ACTIVITY IN THE PLASMA AND UTERUS OF LAYING HENS

1970 ◽  
Vol 64 (3) ◽  
pp. 398-409 ◽  
Author(s):  
N. Snapir ◽  
M. Perek

ABSTRACT In both young and old laying hens the protein-bound calcium fraction in blood plasma decreased following feed supplementation of 0.05% thyroprotein, whereas the plasma alkaline phosphatase activity significantly increased. The enzyme response was found to be delayed in old as compared to young hens, significantly higher absolute levels being found in the latter. Propylthiouracil treatment caused a marked decrease in protein-bound calcium levels and alkaline phosphatase activity in both young and old hens. The uterine calcium levels and alkaline phosphatase activity in the thyroprotein treated birds did not show any significant differences as compared to the controls, except in the group of old hens receiving the highest dose, in which the calcium level was significantly decreased and the enzyme activity significantly increased. Both propylthiouracil treated groups showed a significant decrease in uterine calcium and alkaline phosphatase activity.

1970 ◽  
Vol 64 (4) ◽  
pp. 670-675 ◽  
Author(s):  
M. Perek ◽  
N. Snapir

ABSTRACT The source of increased plasma alkaline phosphatase activity in laying hens following thyroprotein feed supplementation was investigated in the liver, kidney, duodenum, jejunum, ileum, uterus and femur. Enzyme activity was found to be the most responsive in the duodenum and bone; response in the bone was almost twice as high as in the control group. The epiphyseal parts of the bone showed the greatest relative response as compared with the cortical or medullary parts, though the absolute highest activity was found in the latter. It seems, therefore, that the bone serves as the main source of increased plasma alkaline phosphatase activity in hyperthyroid laying hens.


1979 ◽  
Vol 183 (1) ◽  
pp. 73-81 ◽  
Author(s):  
R Felix ◽  
H Fleisch

1. Dichloromethanediphosphonate and to a lesser degree 1-hydroxyethane-1,1-diphosphonate, two compounds characterized by a P-C-P bond, increased the alkaline phosphatase activity of cultured rat calvaria cells up to 30 times in a dose-dependent fashion. 2. Both diphosphonates also slightly inhibited the protein synthesis in these cells. 3. Thymidine, an inhibitor of cell division, did not inhibit the induction of the enzyme, indicating that the increase in enzyme activity was not due to the formation of a specific population of cells with high alkaline phosphatase activity. 4. The effect on alkaline phosphatase was suppressed by the addition of cycloheximide, an inhibitor of protein synthesis. 5. After subculturing the stimulated cells in medium without diphosphonates, the enzyme activity fell almost to the control value. 6. Bovine parathyrin diminished the enzyme activity of the control cells and the cells treated with dichloromethanediphosphonate; however, at high concentration the effect of parathyrin was greater on the diphosphonate-treated cells than on the control cells. 7. The electrophoretic behaviour, heat inactivation, inhibition by bromotetramisole or by phenylalanine, and the Km value of the induced enzyme were identical with that of the control enzyme.


PEDIATRICS ◽  
1953 ◽  
Vol 11 (4) ◽  
pp. 309-322
Author(s):  
EDNA H. SOBEL ◽  
LELAND C. CLARK ◽  
R. PHYLLIS FOX ◽  
MEINHARD ROBINOW

A child, studied between the ages of 1½ and 3½ years, presented an abnormally low plasma alkaline phosphatase activity (0.8-1.64 Bessey-Lowry u.), a deformed skeleton and the loss of most of her deciduous teeth. The serum Ca was normal; the serum inorganic phosphate remained at the normal relatively high levels of infancy as the child grew older Roentgenograms demonstrated deficient mineralization of the skeleton and teeth. Biopsies of the liver and the costochondral junction displayed a deficiency of tissue alkaline phosphatase activity. The architecture of the rib was consistent with rickets. There was no evidence for the presence of an inhibitor of alkaline phosphatase, such as beryllium, or for an excessive excretion of the enzyme. Treatment with purified growth hormone, ascorbic acid and thiamin chloride had no effect, while vitamin D 500 thousand u. caused little change in the enzyme activity in a 10 day period. The father had low plasma alkaline phosphatase activity and a number of similar patients are mentioned, for whom there was also evidence that the deficiency in alkaline phosphatase activity may be genetically determined. While the precise role of alkaline phosphatase activity in the metabolism of bone is not clear, the findings in this patient suggest that growing bone may require the presence of alkaline phosphatase for normal calcification, and that the skeletal disorder, which could not be distinguished from rickets, may be related to a disturbance in the local factor.


1989 ◽  
Vol 23 (1) ◽  
pp. 53-58 ◽  
Author(s):  
C. S. Thompson ◽  
D. P. Mikhailidis ◽  
D. S. Gill ◽  
J. Y. Jeremy ◽  
J. L. Bell ◽  
...  

The effect of starvation and sampling time on plasma alkaline phosphatase activity, total plasma calcium concentration and whole blood ionized calcium concentration was determined in the rat. Starvation caused a significant fall in total and ionized calcium concentrations as well as in alkaline phosphatase activity. These changes were accompanied by a fall in whole blood pH and an increase in the anion gap and a decrease in urinary excretion of calcium. These indices were restored to normal following refeeding. There was no change in serum 25-OH vitamin D concentrations following starvation for 3 days. Alkaline phosphatase activity showed a pattern compatible with the presence of a circadian rhythm when sampling took place between 0800 and 1800 h. Total and ionized calcium concentrations did not show such a rhythm when animals were fed the present diet.


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