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A fluorescence study of horse plasma gelsolin labelled with 6-acryloyl-2-dimethylaminonapthalene Reid, Scott William
Abstract
Gelsolin was labelled with the sulphydryl-specific fluorescent reagent 6-acryloyl-2-dimethylaminonaphthalene (acrylodan). The degree of labelling using non-denaturing conditions was 1.9 ± 0.5 acrylodans per gelsolin molecule. Circular dichroism and viscosity studies showed no significant effect on gelsolin structure and function on incorporation of the label. Circular dichroism studies did not detect Ca²⁺ effects on aerylodan-labelled gelsolin, but fluorescence studies detected subtle changes in the protein. The presence of Ca²⁺ causes a decrease and red-shift in fluorescence emission, an increase in sensitivity to quenching by I⁻ and a decrease in fluorescence polarisation of the acrylodan-labelled gelsolin. These indicate an increased degree of exposure of the fluorescent label to the solvent environment on interaction of gelsolin with Ca²⁺. Actin binding to gelsolin was evident from a decrease in fluorescence intensity, an increase in sensitivity to quenching and an increase in fluorescence polarisation. Actin binding increases the exposure of the acrylodan label to solvent, as does Ca²⁺ binding.
Item Metadata
Title |
A fluorescence study of horse plasma gelsolin labelled with 6-acryloyl-2-dimethylaminonapthalene
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Creator | |
Publisher |
University of British Columbia
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Date Issued |
1990
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Description |
Gelsolin was labelled with the sulphydryl-specific fluorescent reagent 6-acryloyl-2-dimethylaminonaphthalene (acrylodan). The degree of labelling using non-denaturing conditions was 1.9 ± 0.5 acrylodans per gelsolin molecule. Circular dichroism and viscosity studies showed no significant effect on gelsolin structure and function on incorporation of the label.
Circular dichroism studies did not detect Ca²⁺ effects on aerylodan-labelled gelsolin, but fluorescence studies detected subtle changes in the protein. The presence of Ca²⁺ causes a decrease and red-shift in fluorescence emission, an increase in sensitivity to quenching by I⁻ and a decrease in fluorescence polarisation of the acrylodan-labelled gelsolin. These indicate an increased degree of exposure of the fluorescent label to the solvent environment on interaction of gelsolin with Ca²⁺.
Actin binding to gelsolin was evident from a decrease in fluorescence intensity, an increase in sensitivity to quenching and an increase in fluorescence polarisation. Actin binding increases the exposure of the acrylodan label to solvent, as does Ca²⁺ binding.
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Genre | |
Type | |
Language |
eng
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Date Available |
2010-12-02
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Provider |
Vancouver : University of British Columbia Library
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Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
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DOI |
10.14288/1.0059766
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URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
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Campus | |
Scholarly Level |
Graduate
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Aggregated Source Repository |
DSpace
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Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.