JBC

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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Poole, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Poole, B.
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?

The Kinetics of Disappearance of Labeled Leucine from the Free Leucine Pool and Rat Liver and Its Effect on the Apparent Turnover of Catalase and Other Hepatic Proteins

Brian Poole 1

From the 1 From The Rockefeller University, New York, New York 10021

The specific radioactivity of free leucine has been measured in rat liver at various times after the injection of labeled leucine. The results of these measurements have served to calculate the effect of leucine reutilization on a previous measurement of the apparent turnover rate of catalase with labeled leucine as precursor. This effect was found to account entirely for the difference between the half-life of catalase observed in these experiments (3.5 days) and that determined with dgr-aminolevulinate as precursor or by indirect methods (1.5 days).

It is shown that in general, when the specific radioactivity of proteins is measured between 1 and 10 days after the injection of labeled leucine, all proteins with half-lives between 0.1 and 2 days will show apparent half-lives between 3 and 4 days. The limitations of using leucine for studies on protein turnover are discussed, and some suggestions are made for optimizing the design of such experiments.

Submitted on April 26, 1971


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
J. Biol. Chem.Home page
D. A. Ferrington, A. G. Krainev, and D. J. Bigelow
Altered Turnover of Calcium Regulatory Proteins of the Sarcoplasmic Reticulum in Aged Skeletal Muscle
J. Biol. Chem., March 6, 1998; 273(10): 5885 - 5891.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
J. H. McKerrow and A. B. Robinson
Primary Sequence Dependence of the Deamidation of Rabbit Muscle Aldolase
Science, January 11, 1974; 183(4120): 85 - 85.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1971 by the American Society for Biochemistry and Molecular Biology.