Allowance for thermodynamic non-ideality in the characterization of protein self-association by frontal exclusion chromatography: hemoglobin revisited-Reference-Cited by-同舟云学术

Allowance for thermodynamic non-ideality in the characterization of protein self-association by frontal exclusion chromatography: hemoglobin revisited

Published:2003-05 Issue:1 Volume:104 Page:345-359
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Winzor Donald J,Wills Peter R

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference52 articles.

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2. Studies of chemically reacting systems on Sephadex. 2. Molecular weights of monomers in rapid association equilibrium;Winzor;J. Phys. Chem.,1964

3. Determination of stoichiometry and equilibrium constants for reversibly associating systems by molecular sieve chromatography;Ackers;Proc. Natl. Acad. Sci. USA,1965

4. The sulfatase of ox liver. IX. The polymerization of sulfatase A;Nichol;Biochemistry,1965

5. Molecular sieve studies of interacting systems. I. Equations for transport of associating systems;Ackers;J. Biol. Chem.,1967

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