The Membrane of Leaf Peroxisomes Contains a Porin-like Channel *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 270, Issue: 29, Page: 17559-17565
1995
- 57Citations
- 16Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations57
- Citation Indexes57
- 57
- CrossRef54
- Captures16
- Readers16
- 16
Article Description
Spinach leaf peroxisomes were purified by Percoll density gradient centrifugation. After several freeze-thaw cycles, the peroxisomal membranes were separated from the matrix enzymes by sucrose density gradient centrifugation. The purity of the peroxisomal membranes was checked by measuring the activities of marker enzymes and by using antibodies. Lipid bilayer membrane experiments with the purified peroxisomal membranes, solubilized with a detergent, demonstrated that the membranes contain a channel-forming component, which may represent the major permeability pathway of these membranes. Control experiments with membranes of other cell organelles showed that the peroxisomal channel was not caused by the contamination of the peroxisomes with mitochondria or chloroplasts. The peroxisomal channel had a comparatively small single channel conductance of 350 pS in 1 M KCl as compared with channels from other cell organelles. The channel is slightly anion selective, which is in accordance with its physiological function. The single channel conductance was found to be only moderately dependent on the salt concentration in the aqueous phase. This may be explained by the presence of positive point net charges in or near the channel or by the presence of a saturable binding site inside the channel. The possible role of the channel in peroxisomal metabolism is discussed.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818956486; http://dx.doi.org/10.1074/jbc.270.29.17559; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0029081876&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/7542242; https://linkinghub.elsevier.com/retrieve/pii/S0021925818956486; https://dx.doi.org/10.1074/jbc.270.29.17559
Elsevier BV
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