Purification and Characterization of Malic Enzyme of Entamoeba invadens: Evidence for Isoenzymes*

1 November 1974

journal article
Published by Wiley in The Journal of Protozoology

Vol. 21 (5) , 796-802
https://doi.org/10.1111/j.1550-7408.1974.tb03754.x

Abstract

SYNOPSIS. Malic enzyme (EC 1.1.1.40) of Entamoeba invadens seems to be a single species of protein on zone‐sedimentation, gel filtration, and gel electrophoresis. The molecular weight of the enzyme was estimated to be 120,000 and sedimentation coefficient close to 6S. Isoelectric focusing, however, showed malic enzyme to be composed of three isoenzymes of pI 5.8, 6.0, and 6.3. A procedure is described that yields an electrophoretically pure sample of each of the isoenzymes suitable for physical and chemical studies.

Keywords

This publication has 37 references indexed in Scilit:

ISOELECTRIC FOCUSING AND STUDY OF RIBOSOMAL PROTEINS AND LACTATE DEHYDROGENASE*
Annals of the New York Academy of Sciences, 1973
Purification and properties of L-malic enzyme from Escherichia coli
Biochemistry, 1970
Metabolic and hormonal regulation of phosphopyruvate synthesis
Advances in Enzyme Regulation, 1964
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
Annals of the New York Academy of Sciences, 1964
MALIC ENZYME AND LIPOGENESIS
Proceedings of the National Academy of Sciences, 1964
Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide Gels
Nature, 1962
An electron microscopic study of Entamoeba invadens rodhain 1934
Experimental Cell Research, 1959
THE ROLE OF CO₂ FIXATION IN CARBOHYDRATE UTILIZATION AND SYNTHESIS
Annals of the New York Academy of Sciences, 1959