JBC Oz Biosciences

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 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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tsai, S.-C.
Right arrow Articles by Vaughan, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsai, S.-C.
Right arrow Articles by Vaughan, M.
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?

Inactivation of Hormone-sensitive Lipase from Adipose Tissue with Adenosine Triphosphate, Magnesium, and Ascorbic Acid

Su-Chen Tsai 1, Henry M. Fales 1, and Martha Vaughan 1

From the 1 From the Molecular Disease Branch and Laboratory of Chemistry, National Heart and Lung Institute, National Institutes of Health, Bethesda, Maryland 20014

Inactivation of ammonium sulfate-precipitated lipase requires, in addition to ATP and Mg2+ion, a dialyzable factor present in homogenates of adipose tissue (Tsai, S.-C., and Vaughan, M. (1972) J. Biol. Chem. 247, 6253–6258) and liver which has now been identified as ascorbic acid. It was extracted from acetone powder of rat liver with methanol-water, 70:30, and purified using barium precipitation and ion exchange and paper chromatography. Approximately 3 mg of a fine white powder obtained from 100 g of liver were used for preparation of trimethylsilyl and deuterotrimethylsilyl derivatives with and without prior reaction with diazomethane. Analysis of these with gas chromatography and mass spectrometry led to the conclusion that the factor was ascorbic acid. This was confirmed by analysis of the trimethylsilyl derivative of authentic l-ascorbic acid. The ultraviolet absorption spectrum and chemical characteristics of the isolated material were consistent with this designation.

Lipase inactivation was proportional to ascorbic acid concentration in the range of 0.3 to 3 µm in the presence of 2 mm ATP and 4 mm MgCl2. In the absence of the latter, ascorbic acid, like the inactivation factor, did not alter lipase activity. Identification of ascorbic acid as the tissue factor required for Mg2+ATP-dependent inactivation of the hormone-sensitive lipase should facilitate further characterization of this process. In addition, because the requirement for ascorbic acid appears to be rather specific and the effective concentrations low relative to those employed in many other enzymatic systems, these observations may lead to the demonstration of a role for ascorbic acid in reactions of a type not hitherto associated with this compound.

Submitted on March 29, 1973


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?





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1973 by the American Society for Biochemistry and Molecular Biology.