Use of analytical gel chromatography to analyze tertiary and quaternary structural changes in E. coli aspartate transcarbamylase.

doi:10.1016/0165-022x(90)90073-l

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Article

Use of analytical gel chromatography to analyze tertiary and quaternary structural changes in E. coli aspartate transcarbamylase.

Journal of biochemical and biophysical methods - 1 Jan 1990

Bromberg S, Burz D S, Allewell N M

Abstract excerpt

E. coli aspartate transcarbamylase (ATCase) is a large (310 kDa) protein that undergoes major changes in quaternary structure when substrates and regulatory nucleotides bind. We have used analytical gel chromatography to detect quaternary structure changes in both the holoenzyme and its catalytic...

Topics

Aspartate Carbamoyltransferase
Chromatography, Gel
Escherichia coli
Ligands
Macromolecular Substances
Mutation
Protein Conformation
Protein Denaturation
Structure-Activity Relationship
Urea

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