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Evidence implicating a membrane ATPase in the control of passive permeability of excitable cells

✍ Scribed by K. Bowler; C. J. Duncan

Publisher: John Wiley and Sons
Year: 1967
Tongue: English
Weight: 462 KB
Volume: 70
Category: Article
ISSN: 0021-9541
DOI: 10.1002/jcp.1040700116

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✦ Synopsis

The temperature sensitivity of the ATPase enzyme systems in a muscle microsomal preparation from the crayfish, Astacus pallipes, was studied. Preincubation of the enzyme preparation in the range 33-36°C produced a marked inactivation of the ATPases; the Mg+ +-dependent ATPase was very much more sensitive to this treatment than the Na+-K+-Mg+ +-dependent ATPase. Thus, the Arrhenius p for the inactivation of the Mg++-dependent ATPase produced by eight minute preincubation is > 100 Kcals. These results are compared with the changes that are observed during the heat death of the whole animal, where exposure to 35°C produces a dramatic change in Na+ permeability within five minutes. Arrhenius p for heat death is also > 100 Kcals and operates over the identical critical temperature range. It is suggested that the Mg+ +-dependent ATPase controls passive permeability in these excitable cells and the results also confirm the view that Mg++ and Na+-K+-Mg++ ATPases are separate enzymes.

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