Ionic binding, net charge, and Donnan effect of human serum albumin as a function of pH

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公開日
1993-01-01
権利情報
  • https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model
DOI
  • 10.1093/clinchem/39.1.48
公開者
Oxford University Press (OUP)

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<jats:title>Abstract</jats:title> <jats:p>The ionic activities and total molalities of sodium, potassium, calcium, lithium, and chloride in a solution of human serum albumin were measured at different values of pH between 4 and 9. The same quantities were measured simultaneously in a protein-free electrolyte solution in membrane equilibrium with the albumin solution. Taking the residual liquid-junction potential and bias from unselectivity of the electrodes into account, we determined the own, bound, and net charges of albumin. Chloride was amply bound at low pH, and calcium at high pH. The varying charge of ions bound to albumin opposed the effect of acid or base on the net charge. All ions were distributed across the membrane according to the same electric potential difference, which equalled the Donnan potential. The high concordance between observation and theory favors the Donnan theory and furthermore implies that the electrodes are as accurate in a solution with albumin as in a protein-free solution.</jats:p>

収録刊行物

  • Clinical Chemistry

    Clinical Chemistry 39 (1), 48-52, 1993-01-01

    Oxford University Press (OUP)

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