Circular Dichroism of Bovine Plasma Albumin—Dye complexes
Open Access
- 1 September 1969
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 10 (2) , 274-277
- https://doi.org/10.1111/j.1432-1033.1969.tb00685.x
Abstract
We report on the circular dichroism induced in two dyes, 2,7‐dibromo‐4‐hydroxy mercurifluorescein and pyridoxal‐5‐phosphate, bound to bovine plasma albumin. We show that the optical activity induced in 2,7‐dibromo‐4‐hydroxy mercurifluorescein, covalently bound to the unique sulfhydryl residue of the protein, makes it possible to follow the pH dependent transitions of bovine plasma albumin occurring in the pH ranges 3 to 5 and 6 to 8. The optical activity induced in the dye is important only for the contracted state of the protein obtained near the isoionic point. On the other hand we show that the optical activity induced in pyridoxal‐5‐phosphate, a dye probably bound to the ɛ‐amino group of a particular lysine residue, is independent of pH between pH 5 and 8.Keywords
This publication has 16 references indexed in Scilit:
- Conformation of horse heart ferricytochrome c. III. Comparative optical rotatory dispersion study of the protein with its derivative heme undecapeptideBiopolymers, 1967
- OPTICAL ROTATORY DISPERSION OF HUMAN CARBONIC ANHYDRASES: COTTON EFFECTS AND AROMATIC ABSORPTION BANDSProceedings of the National Academy of Sciences, 1965
- The ultraviolet fluorescent of proteins I. The influence of pH and temperatureBiochimica et Biophysica Acta, 1963
- Optical Rotatory Dispersion of Dyes Bound to Macromolecules. Cationic Dyes: Polyglutamic Acid Complexes2,3Journal of the American Chemical Society, 1961
- Perturbation of the Ultraviolet Absorption Spectrum of Anthracene Coupled to Bovine Plasma Albumin1Journal of the American Chemical Society, 1960
- ANOMALOUS OPTICAL ROTATORY DISPERSION OF DYE: POLYPEPTIDE COMPLEXESProceedings of the National Academy of Sciences, 1959
- An Investigation of Bovine Plasma Albumin by Differential Ultraviolet Spectroscopy1Journal of the American Chemical Society, 1959
- The Hydrogen Ion Equilibria of a Single Group Attached to Serum Albumin: Some Implications as to the Surface Characteristics of Protein MoleculesJournal of the American Chemical Society, 1957
- Interactions of Some Neutral Organic Molecules with ProteinsJournal of the American Chemical Society, 1952
- Structural Specificities in the Interactions of Some Organic Ions with Serum AlbuminJournal of the American Chemical Society, 1952