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September 1, 1970Journal of Biological ChemistryOpen Access

Purification and Properties of an Adenosine Triphosphatase from Sarcoplasmic Reticulum

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Authors

DMDavid H. MacLennanElectrophysiology

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Implication

Randomized trial investigates ATPase properties in sarcoplasmic reticulum, indicating phospholipid's role in activity.

Key Points

  • This research aimed to purify an adenosine triphosphatase from sarcoplasmic reticulum and examine its properties.
  • Purification was achieved using deoxycholate and salt fractionation methods.
  • Gel electrophoresis was utilized to analyze the protein composition and activity.
  • The enzyme was tested for stability and activity in both soluble and insoluble states under various conditions.
  • Purified ATPase showed a six-fold increase in activity compared to initial preparations.
  • Activity required Mg++ and was enhanced by Ca++, but inhibited by specific chelators and mersalyl acid.
  • Phospholipid content was crucial for ATPase activity, as inhibition by phospholipase C could be reversed by adding phospholipid.

Cite This Study

David H. MacLennan (1970) studied this question.

synapsesocial.com/papers/6a22b0ff80ebe3feac149efehttps://doi.org/10.1016/s0021-9258(19)63820-2
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