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The Journal of Cell Biology, Vol 41, 536-546, Copyright © 1969 by Rockefeller University Press

ARTICLE

THE SYNTHESIS AND TURNOVER OF RAT LIVER PEROXISOMES

: II. Turnover of Peroxisome Proteins



Brian Poole 1, Federico Leighton 1, and Christian De Duve 1

1 From the Rockefeller University, New York 10021.

Dr. Poole's present address is Laboratoire de Morphologie Animale, Université Libre de Bruxelles, Belgium. Dr. Leighton's present address is Department of Pathological Physiology, Catholic University of Chile, Santiago, Chile

After preliminary experiments had established that the injection of Triton WR-1339 necessary for the separation of lysosomes and peroxisomes did not affect the turnover rate of catalase, the decay of 3H-leucine incorporated into peroxisomes was studied in whole particles and in protein subfractions. It was shown that peroxisomes are destroyed in a completely random way, probably as wholes since the apparent half-life was the same for all subfractions, about 3frac12 days. In agreement with the results of Price et al. (11), the half-life of catalase derived from the rate of recovery from aminotriazole inhibition was about 11frac12 days, as was the apparent half-life of the heme prosthetic groups measured with 14C-alpha-aminolevulinic acid. Guanidino-labeled arginine gave an apparent half-life of 2frac12 days with large statistical uncertainty. Either the leucine label was reutilized very extensively in our animals and the true half-life of peroxisomes is 1frac12 days, or the prosthetic groups of catalase turn over more rapidly than the protein part of the molecule.

Submitted on October 10, 1968
Revised on December 9, 1968


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