Apr 1, 1976

Spectral properties of porcine plasminogen: study of the acidic transition (author's transl)

European Journal of Biochemistry
F Rodier

Abstract

The acidic transition of porcine plasminogen, prepared by affinity chromatography, was studied by non-destructive methods. These methods are based on the analysis of the behaviour of the tryptophyls under various conditions. The perturbation of the absorption and emission spectra by pH or temperature and the dynamic quenching of the intrinsic fluorescence are used to obtain information on structural changes which affect the environment of these residues. It is shown that by decreasing pH the fluorescence emission spectra are shifted toward the long wavelengths, with a broadening of the fluorescence band. The same effect can be obtained at constant pH by heating the protein solution. In order to analyze these phenomena, it is assumed that the fluorescence intensities at 355 nm and 328 nm reflect the proportion of the tryptophans which are exposed to the solvent, and buried, respectively. The plot of the ratio of the fluorescence intensities at these wavelengths versus pH or temperature leads to a titration curve showing an unmasking of tryptophans. The proportion of exposed tryptophans is measured by the dynamic fluorescence quenching technique and the data analyzed according to Lehrer. The plot of the fraction of exposed trypto...Continue Reading

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Mentioned in this Paper

Tryptophan
Plasminogen Measurement
Inversion Mutation Abnormality
Plasminogen
Fluorescence Spectroscopy
Plasma Protein Binding Capacity
PLG gene
Protein Conformation
Spectrophotometry, Ultraviolet
Aromatics

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