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Solubilization and partial purification of mitochondrial delta-aminolevulinate synthase from fetal rat liver
- Source :
- Biochimica et biophysica acta. 350(1)
- Publication Year :
- 1974
-
Abstract
- A particulate preparation of δ-aminolevulinate synthase (EC 2.3.1.37) from fetal rat liver mitochondria has been rendered soluble by treatment with the non-ionic detergent Lubrol WX-4. A partial purification of the detergent-solubilized enzyme was achieved by gel filtration on Sephadex G-200. Unlike the adult mitochondrial enzyme, δ-aminolevulinate synthase from fetal liver is inhibited by NaCl but not by hemin.
- Subjects :
- Time Factors
Size-exclusion chromatography
Detergents
Mitochondria, Liver
Heme
Biology
Sodium Chloride
chemistry.chemical_compound
Surface-Active Agents
Fetus
Drug Stability
Freezing
Animals
Ultrasonics
chemistry.chemical_classification
ATP synthase
General Medicine
Molecular biology
Kinetics
Enzyme
chemistry
Biochemistry
Solubility
Sephadex
Solubilization
Rat liver
biology.protein
Chromatography, Gel
Female
Ultracentrifugation
Hemin
5-Aminolevulinate Synthetase
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 350
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....daf42a1522cc7abadaed644360c7375a