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Purification and Characterization of Malic Enzyme of Entamoeba invadens : Evidence for Isoenzymes *
Author(s) -
BURO NICHOLAS C.,
WELLER DAVID L.
Publication year - 1974
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1974.tb03754.x
Subject(s) - malic enzyme , enzyme , isozyme , isoelectric focusing , entamoeba , chromatography , isoelectric point , biochemistry , size exclusion chromatography , chemistry , sedimentation coefficient , sedimentation , electrophoresis , molecular mass , microbiology and biotechnology , biology , entamoeba histolytica , sediment , paleontology , dehydrogenase
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.

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