TY  - JOUR
A1  - Reske, Günter
A1  - Nimmerfall, Fritz
A1  - Stauff, Joachim
T1  - Über Photoreaktionen und Lumineszenzverhalten von Eosin in wäßrigen Lösungen von β-Lactoglobulin, Rinderserumalbumin und Cystein
T2  - Zeitschrift für Naturforschung, B
N2  - Interactions of eosin with three different substrates, β-lactoglobuline, bovine serum albumin and cysteine, in aqueous solutions of pH 7 under illumination with light of wavelengths 5200—5400 Å are investigated by changes in absorption spectrum characteristics, SH-group activities and phosphorescence intensities.
Only with bovine serum albumin the major part of protein conversion, as shown by spectral changes and diminution of SH-groups due to eosin-sensitized photo-oxidation. In β-lactoglobuline an oxidizing photoreaction occurs, by which eosin is vanishing to the same degree as the protein shows loss of SH-groups and spectral alterations indicating attack on aromatic amino acid residues. There is no red shift of the eosin absorption band at 5170 Å as is observed in solutions of bovine serum albumin, where the intensity of phosphorscence is about 100 fold compared with the intensity obtained by solutions of β-lactoglobulin.
The aerobic eosin photoreaction in solutions of β-lactoglobulin is faster than aerobic photobleaching of the dye. Still faster is its bleaching photoreaction with cysteine, which is nearly independent of oxygen.
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/71394
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-713945
SN  - 1865-7117
SN  - 0932-0776
VL  - 21
IS  - 4
SP  - 305
EP  - 313
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -