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 Nakanishi, Y.
Right arrow Articles by Isohashi, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakanishi, Y.
Right arrow Articles by Isohashi, F.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1994, Vol. 115, No. 2 328-332
© 1994 Japanese Biochemical Society

research-article

Subcellular Distribution of ATP-Stimulated and ADP-Inhibited Acetyl-CoA Hydrolase in Livers from Control and Clofibrate-Treated Rats: Comparison of the Cytosolic and Peroxisomal Enzyme1

Yoko Nakanishi2, Kazuki Okamoto and Fumihide Isohashi3

Division of Biochemistry, Department of Oncology, Biomedical Research Center, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565

3 To whom correspondence should be addressed.

An extramitochondrial acetyl-CoA hydrolase [EC 3.1.2.1 [EC] ] in the rat liver, which is stimulated by ATP and inhibited by ADP, is known to be extremely cold-labile. During subcellular fractionations at low temperatures (2–4°C), most of the enzyme activity was lost; however, most could be recovered by rewarming at 37°C in the presence of a high concentration of potassium phosphate. This enabled us to measure the activities of cold-treated samples. The majority of the ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase activity in rat livers was detected in the cytosolic fraction and small amounts were detected in the peroxisomal fraction. The activity of peroxisomal ATP-stimulated acetyl-CoA hydrolase was not noticeably increased after clofibrate-treatment. However, the cytosolic activity greatly increased after clofibrate treatment. The activity in the isolated peroxisomal fraction per g of liver was about 5% of that in the cytosolic fraction of liver from the control and about 2% in that from clofibrate-treated rats. Besides having similar nucleotide (ATP and ADP) sensitivity and cold lability, the enzyme protein in the peroxisomal fraction migrated to the same position as the cytosolic acetyl-CoA hydrolase based on Western blot analysis with antibody against purified acetyl-CoA hydrolase from rat liver cytosol. These results suggest that the peroxisomal enzyme and cytosolic enzyme may be the same entity.

1This work was supported by grants from the Japan Foundation for Applied Enzymology and the Vitamin Society of Japan and by a Grant-m-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.

2Present address: Department of Home Economics, Kyoto University of Education, Fukakusafujinomori 1, Fushimi-ku, Kyoto, Kyoto 612.


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




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.