Demonstration, by renaturation in O'Farrell gels, of heterogeneity in Dictyostelium uridine diphosphoglucose pyrophosphorylase |
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| Authors: | R E Manrow R P Dottin |
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| Institution: | Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218 USA |
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| Abstract: | A new procedure has been devised for the rapid isolation of yeast hexokinase isoenzymes PI and PII, giving specific activities comparable to those obtained after conventional purification. Hexokinases were bound to d-glucosamine, which had been coupled to CH Sepharose 4B using 6-aminohexanoic acid as a spacer. An ATP/d-glucose/MgCl2 solution was used for elution. After concentration with DEAE-Sephacel, isoenzymes were separated by chromatofocusing. Hexokinase PI gave a single band on polyacrylamide gel electrophoresis, whereas one minor foreign band was seen for hexokinase PII. |
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| Keywords: | To whom reprint requests should be addressed |
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