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Purification of yeast hexokinase isoenzymes using affinity chromatography and chromatofocusing

โœ Scribed by E. Kopetzki; K.-D. Entian

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
297 KB
Volume
121
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

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/MgC& 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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