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Collect. Czech. Chem. Commun. 1996, 61, 808-818
https://doi.org/10.1135/cccc19960808

Picosecond Tryptophan Fluorescence of Human Blood Serum Orosomucoid

Martin Hofa, Stefan Vajdab, Vlastimil Fidlerc and Vladimír Karpenkoa

a Department of Physical Chemistry, Charles University, 128 40 Prague 2, Czech Republic
b Department of Chemical Physics, Charles University, 121 16 Prague 2, Czech Republic
c Department of Physical Electronics, Czech Technical University, 180 00 Prague 8, Czech Republic

Crossref Cited-by Linking

  • Albani Jihad R., Bretesche Loïc, Vogelaer Julie, Kmiecik Daniel: Energy Transfer Studies between Trp Residues of Three Lipocalin Proteins Family, α1-Acid Glycoprotein, (Orosomucoid), β-Lactoglobulin and Porcine Odorant Binding Protein and the Fluorescent Probe, 1-Aminoanthracene (1-AMA). J Fluoresc 2015, 25, 167. <https://doi.org/10.1007/s10895-014-1493-x>
  • Kmiecik Daniel, Albani Jihad René: Effect of 1-Aminoanthracene (1-AMA) Binding on the Structure of Three Lipocalin Proteins, the Dimeric β Lactoglobulin, the Dimeric Odorant Binding Protein and the Monomeric α1-Acid Glycoprotein. Fluorescence Spectra and Lifetimes Studies. J Fluoresc 2010, 20, 973. <https://doi.org/10.1007/s10895-010-0643-z>
  • Albani J.R.: Progesterone binding to the tryptophan residues of human α1-acid glycoprotein. Carbohydrate Research 2006, 341, 2557. <https://doi.org/10.1016/j.carres.2006.07.012>
  • Albani Jihad René: Effect of the Secondary Structure of Carbohydrate Residues of α1‐Acid Glycoprotein (Orosomucoid) on the Local Dynamics of Trp Residues. Chemistry & Biodiversity 2004, 1, 152. <https://doi.org/10.1002/cbdv.200490007>
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  • Albani Jihad R: Relation between the secondary structure of carbohydrate residues of α1-acid glycoprotein (orosomucoid) and the fluorescence of the protein. Carbohydrate Research 2003, 338, 1097. <https://doi.org/10.1016/S0008-6215(03)00075-2>
  • Albani Jihad R.: Förster energy-transfer studies between Trp residues of α1-acid glycoprotein (orosomucoid) and the glycosylation site of the protein. Carbohydrate Research 2003, 338, 2233. <https://doi.org/10.1016/S0008-6215(03)00360-4>
  • Hofbauerová Kateřina, Kopecký Jr Vladimı́r, Sýkora Jan, Karpenko Vladimı́r: Thermal stability of the human blood serum acid α1-glycoprotein in acidic media. Biophysical Chemistry 2003, 103, 25. <https://doi.org/10.1016/S0301-4622(02)00231-4>
  • De Ceukeleire Melanie, René Albani Jihad: Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and progesterone. A fluorescence study. Carbohydrate Research 2002, 337, 1405. <https://doi.org/10.1016/S0008-6215(02)00165-9>
  • Cogswell Lawrence P., Raines Douglas E., Parekh Sonali, Jonas Oliver, Maggio John E., Strichartz Gary R.: Development of a novel probe for measuring drug binding to the F1*S variant of human alpha 1‐acid glycoprotein. Journal of Pharmaceutical Sciences 2001, 90, 1407. <https://doi.org/10.1002/jps.1093>
  • Albani Jihad R: Effect of binding of Calcofluor White on the carbohydrate residues of α1-acid glycoprotein (orosomucoid) on the structure and dynamics of the protein moiety. A fluorescence study. Carbohydrate Research 2001, 334, 141. <https://doi.org/10.1016/S0008-6215(01)00169-0>
  • Hof M., Häfner A., Merola F., Duportail G., Hutterer R., Schneider F. W.: Calcium-induced conformational change in fragment 1-86 of factor X. Biopolymers (Biospectroscopy) 2000, 57, 226. <https://doi.org/10.1002/1097-0282(2000)57:4<226::AID-BIP4>3.0.CO;2-I>
  • Häfner A., Merola F., Duportail G., Hutterer R., Schneider F. W., Hof M.: Calcium-induced conformational change in fragment 1-86 of factor X. Biopolymers 2000, 57, 226. <https://doi.org/10.1002/1097-0282(2000)57:4<226::AID-BIP4>3.0.CO;2-I>