Purification of phosphotransacetylase by affinity chromatography. |
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Authors: | L T Smith N O Kaplan |
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Affiliation: | University of California—San Diego, Department of Chemistry, Q-058, La Jolla, California 92093 USA |
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Abstract: | Phosphotransacetylase from Clostridium kluyveri was purified using a C8-(6-aminohexyl)-amino-desulfo-coenzyme A-Sepharose column. The method of synthesis of the affinity matrix is described. A crude extract was treated with ammonium sulfate and chromatographed on the desulfo-coenzyme A-Sepharose column. Using this method the enzyme was purified 83-fold and was found to be 73% pure. A new method for the determination of the purity of phosphotransacetylase by activity staining of polyacrylamide gels with 5,5′-dithiobis(2-nitrobenzoic acid) is described. |
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