Thermodynamics and kinetics of the neutral transition of human serum albumin, monitored by the spectral change of bound bilirubin
- 1 May 1980
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 623 (1) , 199-207
- https://doi.org/10.1016/0005-2795(80)90021-5
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Conformational changes in human serum albumin around the neutral pH from circular dichroic measurementsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Bilirubin Acidity. Titrimetric and 13C NMR Studies.Acta Chemica Scandinavica, 1979
- Kinetics of the binding of bilirubin to human serum albumin studied by stopped-flow techniqueArchives of Biochemistry and Biophysics, 1977
- Fluorescence and stopped-flow studies on the N ∡ F transition of serumalbuminBiophysical Chemistry, 1975
- Neutral transition and the environment of the sulfhydryl side chain of bovine plasma albuminBiochemistry, 1974
- Spectral characteristics of bilirubin-bovine albumin complexesClinica Chimica Acta; International Journal of Clinical Chemistry, 1973
- pK change of imidazole groups in bovine serum albumin due to the conformational change at neutral pHBiochemistry, 1971
- Binding of bilirubin to human serum albumin — determination of the dissociation constantsFEBS Letters, 1969
- Optical rotation and viscosity of native and denatured proteins. XII. Differences between human and bovine albuminsArchives of Biochemistry and Biophysics, 1958
- Preparation and Properties of Serum and Plasma Proteins. XXIII. Hydrogen Ion Equilibria in Native and Modified Human Serum Albumins1a, 1bJournal of the American Chemical Society, 1950