J. Lipid Res. Please sign the JLR Guestbook
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tsujita, T.
Right arrow Articles by Okuda, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsujita, T.
Right arrow Articles by Okuda, H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Journal of Lipid Research, Vol 34, 1773-1781, Copyright © 1993 by Lipid Research, Inc.

ARTICLES

Palmitoyl-coenzyme A hydrolyzing activity in rat kidney and its relationship to carboxylesterase

T Tsujita and H Okuda
Department of Medical Biochemistry, School of Medicine, Ehime University, Japan.

Palmitoyl-coenzyme A (palmitoyl-CoA) hydrolase was obtained from rat kidney in an electrophoretically homogeneous form. The enzyme associated with carboxylesterase activity was purified by acetone precipitation of microsomes, followed by successive chromatographies on DEAE-cellulose, phenyl-Sepharose, and Sephadex G-100 gel. The two activities in rat kidney were associated as judged by their co-elution profiles, co-purification at different steps, co-precipitation by an antibody raised against the purified enzyme, and identical profiles of inhibition by diisopropylfluorophosphate. The enzyme catalyzed the hydrolysis of long- and medium-chain acyl-CoA, but not short-chain acyl- CoA. The N-terminal amino acid sequence of the first 27 residues of the purified enzyme was 80% identical with that of the carboxylesterase from rat adipose tissue. Using a polyclonal rabbit antibody against the rat kidney palmitoyl-CoA hydrolase, the enzyme was demonstrated in liver but not in adipose tissue. The antibody reacted with the carboxylesterase(s) (pI 6.3 and pI 6.6) in rat liver microsomes. The antibody removed the palmitoyl-CoA hydrolase in kidney (75%) and liver (68%). The antibody also removed the monoolein hydrolase in kidney (77%) and liver (61%). These results suggest that carboxylesterase contributes to the hydrolysis of long-chain acyl-CoA and monoglyceride in kidney and liver.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 EndocrinologyHome page
C. De Vriese, F. Gregoire, R. Lema-Kisoka, M. Waelbroeck, P. Robberecht, and C. Delporte
Ghrelin Degradation by Serum and Tissue Homogenates: Identification of the Cleavage Sites
Endocrinology, November 1, 2004; 145(11): 4997 - 5005.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
T. Imai, Y. Yoshigae, M. Hosokawa, K. Chiba, and M. Otagiri
Evidence for the Involvement of a Pulmonary First-Pass Effect via Carboxylesterase in the Disposition of a Propranolol Ester Derivative after Intravenous Administration
J. Pharmacol. Exp. Ther., December 1, 2003; 307(3): 1234 - 1242.
[Abstract] [Full Text] [PDF]

Home page
 Pharmacol. Rev.Home page
J. W. Lohr, G. R. Willsky, and M. A. Acara
Renal Drug Metabolism
Pharmacol. Rev., March 1, 1998; 50(1): 107 - 142.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1993 by the American Society for Biochemistry and Molecular Biology.