Journal article
Malate dehydrogenase: Isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms
Bioscience reports, Vol.1(6), pp.497-507
06/01/1981
DOI: 10.1007/BF01121583
PMID: 7028159
Abstract
Escherichia coli malate dehydrogenase has been isolated in homogeneous form by a procedure employing chromatography on DEAE-cellulose, 5′-AMP-Sepharose, and Sephacryl-200. It is composed of two identical polypeptide chains each of Mr = 32 500. Like porcine mitochondrial malate dehydrogenase, it is devoid of tryptophan, but otherwise it is not particularly more similar in composition to one of the eukaryotic isozymes than to the other. However, amino-terminal sequence analysis of the first 36 residues shows remarkable similarity of the bacterial and mitochondrial enzymes (69% identical residues) in contrast to the cytoplasmic form (27%). The two porcine heart enzymes are identical in 24t% of the positions compared. These results clearly establish that all three forms of malate dehydrogenase have evolved from a common precursor and that the prokaryotic and mitochondrial forms have retained sequences that are much closer to the ancestral one than the cytoplasmic enzyme. These findings appear to further substantiate the endosymbiotic hypothesis for the origin of the mitochondrion.
Details
- Title: Subtitle
- Malate dehydrogenase: Isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms
- Creators
- Ross T Fernley - Department of Biological Chemistry, Washington University School of Medicine, St. Louis, MO 63110, U.S.A., Howard Florey Institute for Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria 3052, AustraliaSteven R Lentz - Department of Biological Chemistry, Washington University School of Medicine, St. Louis, MO 63110, U.S.ARalph A Aradshaw - Department of Biological Chemistry, Washington University School of Medicine, St. Louis, MO 63110, U.S.A
- Resource Type
- Journal article
- Publication Details
- Bioscience reports, Vol.1(6), pp.497-507
- DOI
- 10.1007/BF01121583
- PMID
- 7028159
- ISSN
- 0144-8463
- eISSN
- 1573-4935
- Language
- English
- Date published
- 06/01/1981
- Academic Unit
- Hematology, Oncology, and Blood & Marrow Transplantation; Internal Medicine
- Record Identifier
- 9984094620302771
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