Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by FURUNO, K.
Right arrow Articles by KATO, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by FURUNO, K.
Right arrow Articles by KATO, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1982, Vol. 91, No. 6 1943-1950
© 1982 Japanese Biochemical Society

research-article

Isolation and Characterization of Autolysosomes which Appeared in Rat Liver after Leupeptin Treatment

Koji FURUNO, Faculty of Pharmaceutical Sciences, Toyoko ISHIKAWA, Faculty of Pharmaceutical Sciences and Keitaro KATO, Faculty of Pharmaceutical Sciences

Kyushu University Higashi-ku, Fukuoka, Fukuoka 812

Autolysosomes were isolated from rat livers treated with leupeptin by a combination of differential and Percoll density gradient centnfugation techniques. The purified autolysosome fraction was verified by morphological analysis to be highly purified and to contain contaminants which were scarcely detectable. The enrichment of the lysosomal enzyme activities in the purified autolysosomes over the homogenate was 12-, 14-, 22-, and 24-fold for ß-glucuronidase, acid phosphatase, ß-N-acetyl-glucosaminidase, and cathepsin D, respectively. Measurement of the activity of the marker enzymes for various subcellular organelles also proved that the purified autolysosome fraction was essentially free from contamination by other organelles. When the autolysosomes isolated from rat livers treated with leupeptin for 1 h were disrupted by osmolysis, acid hydrolases were easily solubilized. Acid phosphatase, however, became membrane bound in the autolysosomes prepared at longer periods of time after the leupeptin treatment. The autolysosomes exhibited enhanced permeability of the membranes after a short duration of time after the leupeptin treatment (30 and 60 min) and became stabilized later. These changes in the properties of the autolysosomes with time after the leupeptin treatment may be interpreted as meaning that progressive rearrangement of the lysosomal constituents occurred within the autolysosomes with time after the genesis.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
M. Hariri, G. Millane, M.-P. Guimond, G. Guay, J. W. Dennis, and I. R. Nabi
Biogenesis of Multilamellar Bodies via Autophagy
Mol. Biol. Cell, January 1, 2000; 11(1): 255 - 268.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
T. Ueno, K. Ishidoh, R. Mineki, I. Tanida, K. Murayama, M. Kadowaki, and E. Kominami
Autolysosomal Membrane-associated Betaine Homocysteine Methyltransferase. LIMITED DEGRADATION FRAGMENT OF A SEQUESTERED CYTOSOLIC ENZYME MONITORING AUTOPHAGY
J. Biol. Chem., May 21, 1999; 274(21): 15222 - 15229.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.