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B6db references: 79194176

type Journal Article
authors Paterniti, J. R., Jr.; Beattie, D. S.
title delta-Aminolevulinic acid synthetase from rat liver mitochondria. Purification and properties
journal J Biol Chem
ui 79194176
year (1979)
volume 254
number 13
pages 6112-8.
keywords 5-Aminolevulinate Synthetase/*isolation & purification/metabolism
abstract delta-Aminolevulinic acid synthetase has been purified from liver mitochondria of young, uninduced rats. After nonionic detergent solubilization of mitochondrial inner membrane-matrix fractions, the enzyme was purified to a specific activity of approximately 2,000 nmol of delta-aminolevulinic acid formed/h/mg of protein at 30 degrees C, by means of ammonium sulfate precipitation, diethylaminoethyl cellulose chromatography, Sephacryl chromatography, and preparative gel electrophoresis. The purified enzyme preparation thus obtained was apparently homogeneous as judged by its migration as a single band with a molecular weight of 58,000 +/- 6,000 upon electrophoresis in sodium dodecyl sulfate polyacrylamide gels. The native enzyme probably exists as a dimer with a molecular weight of approximately 120,000. A pH optimum of 7.5 and an isoelectric point of 4.5 were also determined. Both monovalent cations and hemin strongly inhibited the activity of the purified enzyme.
last changed 2002/11/04 17:41

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