AJP - Endo Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Endocrinol Metab 244: E101-E107, 1983;
0193-1849/83 $5.00
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yedgar, S.
Right arrow Articles by Steinberg, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yedgar, S.
Right arrow Articles by Steinberg, D.

AJP - Endocrinology and Metabolism, Vol 244, Issue 1 101-E107, Copyright © 1983 by American Physiological Society


ARTICLES

Tissue sites of catabolism of albumin in rabbits

S. Yedgar, T. E. Carew, R. C. Pittman, W. F. Beltz and D. Steinberg

The sites of albumin catabolism were determined in rabbits using [14C]sucrose-labeled rabbit albumin. The [14C]sucrose moiety is not degradable and accumulates in tissues degrading the protein. Albumin was labeled with [14C]sucrose, and the monomeric form was selected for injection into rabbits. The validity of the sucrose-labeled albumin as a tracer for native albumin was shown by the similar plasma decay kinetics of 125I-labeled albumin derivatized with sucrose and 131I-labeled native albumin and by the similar decay kinetics for the biologically screened and unscreened preparations of [14C]sucrose-albumin. Two days after injection of [14C]sucrose-albumin, tissues were assayed for accumulated 14C-labeled degradation products soluble in trichloroacetic acid. All tissues catabolized albumin with no tissue of predominant importance; liver, kidney, and muscle were the largest contributors. Expressed in terms of activity per unit wet weight, adrenal, kidney, spleen, ovary, bone marrow, and liver were the most active. These most active tissues are those with fenestrated or discontinuous capillary beds, suggesting that exposure to high concentrations of albumin is an important determinant of their high rates of albumin degradation.


This article has been cited by other articles:


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
M. Koltun, J. Nikolovski, K. Strong, D. Nikolic-Paterson, and W. D. Comper
Mechanism of hypoalbuminemia in rodents
Am J Physiol Heart Circ Physiol, April 1, 2005; 288(4): H1604 - H1610.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Endocrinol. Metab.Home page
A. L. Sunehag and M. W. Haymond
Maternal protein homeostasis and milk protein synthesis during feeding and fasting in humans
Am J Physiol Endocrinol Metab, August 1, 2003; 285(2): E420 - E426.
[Abstract] [Full Text] [PDF]


Home page
Br J AnaesthHome page
J. P. Nicholson, M. R. Wolmarans, and G. R. Park
The role of albumin in critical illness
Br. J. Anaesth., October 1, 2000; 85(4): 599 - 610.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
K. W. Huggins, E. R. Burleson, J. K. Sawyer, K. Kelly, L. L. Rudel, and J. S. Parks
Determination of the tissue sites responsible for the catabolism of large high density lipoprotein in the African green monkey
J. Lipid Res., March 1, 2000; 41(3): 384 - 394.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online