Serum albumin binding sites properties in donors and in schizophrenia patients: the study of fluorescence decay of the probe K-35 using S-60 synchrotron pulse excitation
Ta. Gryzunov et al., Serum albumin binding sites properties in donors and in schizophrenia patients: the study of fluorescence decay of the probe K-35 using S-60 synchrotron pulse excitation, NUCL INST A, 448(1-2), 2000, pp. 478-482
The properties of serum albumin obtained from donors and from paranoid schi
zophrenia patients were studied with the fluorescent probe K-35 (N-carboxyp
henylimide of dimethylaminonaphthalic acid) and time-resolved fluorescence
spectroscopy on the SR beam station of the S-60 synchrotron of the Lebedev
Physical Institute. The mean fluorescence quantum yield of K-35 in patients
serum was decreased significantly by 25-60% comparing with donors. The ana
lysis of pre-exponential factors of fluorescence decay using "amplitude sta
ndard" method has shown that in patient sera the fraction of K-35 molecules
bound with albumin and inaccessible to fluorescence quenchers ("bright" K-
35 molecules with tau(1) = 8.0 +/- 0.4 ns) is 1.2-3 times less than in the
donor sera. The fraction of K-35 molecules with partly quenched fluorescenc
e (tau(2) = 1.44 +/- 0.22 ns) was significantly increased in schizophrenia
patients. The results obtained suggest that the properties of binding regio
n in serum albumin molecules of acute paranoid schizophrenia patients chang
e significantly. (C) 2000 Elsevier Science B.V. All rights reserved.