The drug binding site of human α1-acid glycoprotein: Insight from induced circular dichroism and electronic absorption spectra

2007 ◽  
Vol 1770 (5) ◽  
pp. 797-809 ◽  
Author(s):  
Ferenc Zsila ◽  
Yasunori Iwao
Keyword(s):  
Circular Dichroism ◽  
Binding Site ◽  
Absorption Spectra ◽  
Electronic Absorption ◽  
Electronic Absorption Spectra ◽  
Drug Binding ◽  
Induced Circular Dichroism ◽  
Acid Glycoprotein ◽  
Drug Binding Site ◽  
Circular Dichroïsm

scholarly journals Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal

1986 ◽  
Vol 233 (1) ◽  
pp. 107-110 ◽  
Author(s):  
J Peterson ◽  
C Godfrey ◽  
A J Thomson ◽  
G N George ◽  
R C Bray
Keyword(s):  
Circular Dichroism ◽  
Low Temperature ◽  
Xanthine Oxidase ◽  
Absorption Spectra ◽  
Magnetic Circular Dichroism ◽  
Electronic Absorption Spectra ◽  
Visible Region ◽  
Absorption Bands ◽  
Magnetic Circular Dichroism Spectroscopy ◽  
Circular Dichroïsm

The magnetic circular-dichroism (m.c.d.) spectra in the temperature range 1.5-100 K and the electronic absorption spectra at 4.2 and 295 K were measured for a number of desulpho xanthine oxidase derivatives. There were no significant differences between the absorption spectra that could be attributed to molybdenum. However, the visible-region m.c.d. spectrum of the ethanediol-treated metalloprotein (which gives rise to the Desulpho Inhibited e.p.r. signal) contained features assignable to Mo(V) absorption bands. This is the first report of the detection of optical bands of Mo(V) in an enzyme in the presence of other chromophoric centres.

Sign in / Sign up

Export Citation Format

Share Document