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  • 1965-1969  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— A comparison was made between K+-Mg2+ activated p-nitrophenyl phosphatase and Na+-K+-Mg2+ activated adenosine triphosphatase with a solubilized enzyme preparation from a membrane fraction of cerebral cortex. The NPPase showed activity even in the absence of phospholipid, whereas the ATPase required the lipid for its activity. More varied types of phospholipids were effective in activating the NPPase than the ATPase, and with each phospholipid the extent and the pattern of the NPPase activation differed from that of the ATPase. By deoxycholate treatment the pH optimum of the NPPase was shifted independently from the pH optimum shift of the ATPase. The specific activity ratio of the NPPase to the ATPase was not constant during purification. These two enzymes were, however, not separable with ammonium sulphate fractionation, and their thermo-lability was identical regardless of the presence of phospholipid. The results suggested two possibilities: (1) the NPPase is a separate enzyme entity from the ATPase; (2) although the NPPase is a part of the ATPase system, the mechanism of action of lipids on the former part differs from that on the rest of the system.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 16 (1969), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Three different types of p-nitrophenyl phosphatases (NPPases) were solubilized by deoxycholate treatment from a membrane fraction of bovine cerebral cortex, and their characteristics were determined. Of these three NPPases (acid, Mg2+-activated, and K+, Mg2+-activated), only K-Mg NPPase was stimulated about two-fold by phospholipid and was inhibited by unsaturated neutral lipids and fatty acids. Unlike Na+-K+-Mga+-activated ATPase, the enzyme did not absolutely require phospholipid for its activity, but was similarly thermolabile and was protected by phospholipid from thermal inactivation. Acid NPPase was separable from the other two NPPases by ammonium sulphate fractionation, and partly solubilized by dialysis against ATP-mercaptoethanol solution. Hg2+ inhibited equally all three NPPases, but Ca2+ inhibited only Mg and K-Mg NPPases. Ouabain was effective on K-Mg NPPase alone.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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