QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Harris, W. R. Articles by Keen, C. Search for Related Content PubMed PubMed Citation Articles by Harris, W. R. Articles by Keen, C.

Calculations of the Distribution of Zinc in a Computer Model of Human Serum¹

Department of Chemistry, University of Missouri, St. Louis, MO 63121 ^* Department of Nutrition, University of California, Davis, CA 95616

During the last decade, investigators employing a wide variety of separation techniques have reported that serum albumin, rather than serum transferrin, is the major carrier protein for labile zinc. However, in contrast to these studies, a simple comparison of the zinc binding constants for albumin and transferrin suggests a significant role for transferrin with regard to serum zinc transport. In the present study multicomponent equilibrium calculations that incorporate recently determined binding constants for zinc-transferrin as well as equilibrium constants for the binding of bicarbonate, sulfate and phosphate to apotransferrin have been used to model the distribution of labile zinc in normal human serum. Anion binding has a major impact on the predicted zinc distribution, lowering the percentage of zinc bound to transferrin from 56% to 11%. The model gives 1% zinc as low-molecular-weight complexes. The improved model results are in good agreement with biological studies on the distribution of zinc among serum proteins.

KEY WORDS: • zinc • species distribution • transferrin • (ECCLES) mathematical model • humans • serum

¹ Financial support for this research was provided by the U.S. Department of Energy contract #DE-AB03-765F00472 via a subcontract from the Laboratory for Energy Related Health Research, University of California, Davis, CA 95616.

Manuscript received 17 March 1989. Revision accepted 11 August 1989.

This article has been cited by other articles:

				F Oakley, N. M Horn, and A. L Thomas Histidine-stimulated divalent metal uptake in human erythrocytes and in the erythroleukaemic cell line HEL.92.1.7 J. Physiol., December 1, 2004; 561(2): 525 - 534. [Abstract] [Full Text] [PDF]