Purification of Isocitrate Lyase fromEscherichia Coltand Watermelon using Fast Protein Liquid Chromatography
- 1 December 1988
- journal article
- research article
- Published by Taylor & Francis in Preparative Biochemistry
- Vol. 18 (4) , 431-442
- https://doi.org/10.1080/00327488808062542
Abstract
The enzyme isocitrate lyase has been purified to gel electrophoretic homogeneity from Escherichia coli and watermelon. From cotyledons of the latter source, the enzyme is obtained in less than 8 hours after precipitation with (NH4)2 SO4 followed by fractionation on cationic Mono S microbeads and anionic Mono Q microbeads using Fast Protein Liquid Chromatography (FPLC). From a genetically engineered E. coli strain, in which high-level expression of isocitrate lyase occurs, the enzyme has been purified in one step from the high-speed supernatant using a Mono Q column with FPLC. These purifications, both of which give satisfactory yields, potentiate rapid access to isocitrate lyase from both prokaryotic and euicaryotic sources.This publication has 21 references indexed in Scilit:
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