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Pharmaceutisch Weekblad

, Volume 5, Issue 5, pp 228–233 | Cite as

Allosteric properties of the oxyphenbutazone-human serum albumin complex

  • J. H. M. Dröge
  • L. H. M. Janssen
  • J. Wilting
Original Articles

Abstract

The conformational change of albumin which occurs around physiological pH, the so-called N-B transition, has been studied by measuring the induced circular dichroic signal of the oxyphenbutazone-albumin complex. This N-B transition has been characterized by a set of parameters according to the two-state model of Monod, Wyman and Changeux. The influence of calcium ions on the N-B transition has been interpreted in terms of a change in some of the parameters describing the two-state model,viz. a decrease of the apparent pK value of the histidines and of the apparent allosteric constant of the oxyphenbutazone-albumin complex. This apparent pK change increases with increasing Ca2+ concentration, whereas the apparent allosteric constant approaches a final value at 5 mM Ca2+. From acid-base titration curves of albumin in the presence and in the absence of Ca2+ it could be concluded that in the presence of Ca2+ less histidines are titratable than in the absence of Ca2+. Assuming that these histidines are not involved in the N-B transition it follows that at least four to five histidines are involved in the N-B transition.

Keywords

Calcium Albumin Serum Albumin Histidine Conformational Change 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Bohn, Scheltema & Holkema 1983

Authors and Affiliations

  • J. H. M. Dröge
    • 1
  • L. H. M. Janssen
    • 1
  • J. Wilting
    • 1
  1. 1.Department of Pharmaceutical Chemistry, Subfaculty of PharmacyState University of UtrechtGH UtrechtThe Netherlands

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