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Citrate synthases from the Archaea: Development of a bio-specific, affinity chromatography purification procedure

Abstract
Citrate synthases from both thermophilic and halophilic Archaea have been purified to homogeneity using affinity chromatography on Matrex Gel Red A and elution with a combination of substrate (oxaloacetate) and product (coenzyme A). In a number of cases, purification from cell-extract to protein suitable for N-terminal sequencing can be achieved by this single-step procedure. The method is particularly useful in the rapid purification of a thermophilic archaeal citrate synthase from a cloned gene expressed in a mesophilic host.
Type
Journal Article
Type of thesis
Series
Citation
James, K.D., Russell, R.J.M., Parker, L., Daniel, R.M., Hough, D.W. & Danson, M.J. (1994). Citrate synthases from the Archaea: Development of a bio-specific, affinity chromatography purification procedure. FEMS Microbiology Letters, 119(1-2), 181-185.
Date
1994
Publisher
Wiley
Degree
Supervisors
Rights