Albumin/calcium association at different pH, as determined by potentiometry.
- 1 November 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in Clinical Chemistry
- Vol. 23 (11) , 2122-2126
- https://doi.org/10.1093/clinchem/23.11.2122
Abstract
Calcium binding by albumin was determined potentiometrically at physiological ionic strength and temperature as a function of pH. The binding data indicate at least 30 different binding sites with different association constants and different H+ interaction. One site appears to be responsible for the major binding at physiological pH and substance concentration of free calcium, together with three other sites that bind with less affinity.This publication has 3 references indexed in Scilit:
- Citrate, pyruvate, and lactate contaminants of commercial serum albuminJournal of Lipid Research, 1968
- A graphic method for the determination and presentation of binding parameters in a complex systemAnalytical Biochemistry, 1967
- Determination of equilibrium constants and maximum binding capacities in complexIn vitro systems: I. The mammillary systemBulletin of Mathematical Biology, 1965