Clinical Chemistry AACC Online Job Center
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 41: 1654-1661, 1995;
This Article
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Vorum, H.
Right arrow Articles by Kragh-Hansen, U.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vorum, H.
Right arrow Articles by Kragh-Hansen, U.

Clinical Chemistry, Vol 41, 1654-1661, Copyright © 1995 by American Association for Clinical Chemistry

Calcium ion binding to clinically relevant chemical modifications of human serum albumin

H Vorum, K Fisker, M Otagiri, AO Pedersen and U Kragh-Hansen
Department of Medical Biochemistry, University of Aarhus, Denmark.

Calcium binding to glycated, penicilloylated, acetylated, and normal defatted human serum albumin as well as to mercapt- and nonmercaptalbumin was studied by equilibrium dialysis of radioactive Ca2+. Binding was quantified by five Scatchard constants [ni = 1, (i = 1-4) and n5 = 10]. Glycation resulted in increased k1- and k2-values and unchanged k3-k5-values, whereas penicilloylation increased all five association constants. The increments were greater the more pronounced the modification, and the enhancements caused by penicilloylation were, for the same degree of modification, greater than those produced by glycation. In contrast, acetylation by acetylsalicylate did not affect calcium binding. Likewise, binding to mercapt- and nonmercaptalbumin was the same, a finding showing that the thiol group of cysteine 34 is not important for calcium binding. D-Glucose and penicillin G are known to react with lysine residues of albumin, and the enhancement of binding resulting from glycation or penicilloylation is probably brought about by unspecific electrostatic effects, possibly supplemented by conformational changes of the protein molecule. The relative importance of the three domains of human serum albumin for calcium binding is discussed.


The following articles in journals at HighWire Press have cited this article:


Home page
 MicrobiologyHome page
J. Kim, K. Ahn, S. Min, J. Jia, U. Ha, D. Wu, and S. Jin
Factors triggering type III secretion in Pseudomonas aeruginosa
Microbiology, November 1, 2005; 151(11): 3575 - 3587.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
I. Londono and M. Bendayan
Temporary effects of circulating Amadori products on glomerular filtration properties in the normal mouse
Am J Physiol Renal Physiol, January 1, 2001; 280(1): F103 - F111.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1995 by the American Association for Clinical Chemistry.