QUENCHING OF TRYPTOPHAN FLUORESCENCE IN HUMAN ANTITHROMBIN III BY IODIDE ION
- 1 November 1977
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 10 (5) , 342-348
- https://doi.org/10.1111/j.1399-3011.1977.tb02806.x
Abstract
Iodide is an efficient quencher of antithrombin III intrinsic tryptophan fluorescence. The quenching pattern indicates that about 60% of the tryptophyl fluorescence originates from exposed residues in the multitryptophan-containing protein. In denaturing media all of the tryptophyls are solvent-exposed. The binding of heparin to antithrombin III influences the number of solvent-exposed tryptophan residues. By studying the dependence of the quenching on pH, information regarding the presence of charged residues adjacent to tryptophyls was obtained.Keywords
This publication has 20 references indexed in Scilit:
- Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescenceBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studiesBiochemistry, 1976
- Characterization of human, bovine, and horse antithrombin IIIBiochemistry, 1976
- Purification of antithrombin III by affinity chromatographyThrombosis Research, 1974
- Anticoagulant Action of HeparinNature, 1973
- Topography of mouse 2.5S nerve growth factor. Reactivity of tyrosine and tryptophanBiochemistry, 1973
- Inactivation of Antithrombin III by Fatty AcidsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1972
- Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ionBiochemistry, 1971
- Highly Purified Antithrombin III with Heparin Cofactor Activity Prepared by Disc ElectrophoresisScandinavian Journal of Clinical and Laboratory Investigation, 1968
- Fluorometric Detection of Histidine‐Tryptophan Complexes in Peptides and ProteinsEuropean Journal of Biochemistry, 1967