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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 384 (1980), S. 149-153 
    ISSN: 1432-2013
    Keywords: Inorganic phosphate ; Alkaline phosphatase ; Kidney ; Brush borders
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Alkaline phosphatase activity in renal cortex homogenates and in isolated brush border membrane vesicles was compared with the rates of sodium-dependent transport of inorganic phosphate (Pi) by isolated brush border membranes. Brush border membrane vesicles were isolated from renal cortical homogenates of rats adapted during a period of 5–7 weeks to diets with different dietary contents of Pi (low Pi diet=0.15 g%, high Pi diet=2.0 g%). Alkaline phosphatase activity was not increased in the low Pi diet group as compared to the standard Pi diet group but was reduced in the high Pi diet group. Sodium-dependent transport of Pi was increased 2–3-fold in the low Pi diet group as compared to the standard Pi diet group, whereas transport activity was only unsignificantly decreased in the high Pi diet group. Studying kinetik parameters in the two extreme dietary groups it has been found that these differences are due to alteredV max of the transport activity as well as of alkaline phosphatase activity. TheK m for both activities remained unaltered. Alkaline phosphatase activity and transport of Pi in brush border membrane vesicles were also compared in the presence of EDTA or Zn2+ at concentrations which inhibit alkaline phosphatase activity. Transport of Pi was not affected by the inhibitors even when alkaline phosphatase was inhibited by more than 70% (0.5 mmol/l Zn2+) or completely (0.5 mmol/l EDTA). The experiments suggest that no correlation between alkaline phosphatase activity and transport of Pi exists in isolated brush border membrane vesicles.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-136X
    Keywords: Enzymatic adaptation ; Low temperature ; Intestine ; Antarctic fish ; Pagothenia bernacchii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The enzymatic activity (expressed as milliunits per milligram total proteins) of three intestinal brush-border membrane enzymes, leucine aminopeptidase, alkaline phosphatase and maltase, measured over a range of temperatures between 1.5 and 37 °C, has been found to be much higher in the Antarctic fish Pagothenia bernacchii than in the temperate fish Anguilla anguilla. To explain this experimental observation the apparent Michaelis-Menten constant, the maximal velocity, the activation energy values and the thermal stability of these three enzymes were measured. The apparent Michaelis-Menten constant values of leucine amino peptidase and alkaline phosphatase were different in the intestine mucosal homogenate of the two fish at each measured temperature (from a minimum of 2.5 to a maximum of 37 °C). However, the values found at 2.5 °C for the Antarctic species and 15 °C for the eel where comparable. Furthermore, its value was unchanged in eel intestine apical membranes, both in the presence and without enzyme lipid microenvironment. While the maximal enzymatic activities of the leucine aminopeptidase and maltase did not decrease without their enzyme lipid microenvironment, produced by treatment with Triton X-100, the impairment of alkaline phosphatase maximal activity cannot be significantly differentiated from a non-specific inhibitory effect of the detergent. The activation energy values of leucine amino peptidase, alkaline phosphatase and maltase were lower in the Antarctic fish (11.7, 5.6 and 11.8 kcal·mol-1, respectively) than in the eel (13.6, 7.6 and 13.1 kcal·mol-1, respectively). The thermal stability of alkaline phosphatase and maltase is different in Pagothenia bernacchii and Anguilla anguilla intestinal homogenate.
    Type of Medium: Electronic Resource
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