The Journal of Membrane Biology

, Volume 34, Issue 1, pp 247–261 | Cite as

Membranous localization and properties of ATPase of rat liver lysosomes

  • Donald L. Schneider
Article
Received:
Revised:

Summary

Lysosomes isolated from rat liver were found to have ATPase activity (EC No. 3.6.1.3). Subfractionation of the lysosomes revealed a membranous localization of ATPase activity. The enzyme has half maximal activity at 0.2mm ATP and is inhibited by high concentrations of ATP. The apparentK m for divalent metal is 0.2mm, and either ca2+ or Mg2+ give maximal activity.

The ATPase activity has latency when lysosomes are isolated from rats treated with Triton WR-1339. This latency may be due to the presence of internalized sucrose because the activity ofL fraction lysosomes is much less latent and Triton WR-1339 itself is not inhibitory. The latency of glucosamindase, a marker enzyme for lysosomes, contrasts with the low latency of the ATPase and points to an ATPase with an exposed active site in intact lysosomes.

Keywords

Sucrose Human Physiology ATPase Activity Maximal Activity Divalent Metal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer-Verlag New York Inc. 1977

Authors and Affiliations

  • Donald L. Schneider
    • 1
  1. 1.Department of BiochemistryUniversity of MassachusettsAmherst

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