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Studies on the substrate binding sites of the pigeon liver fatty acid synthetase
- Source :
- Archives of biochemistry and biophysics. 124(1)
- Publication Year :
- 1968
-
Abstract
- Data are presented on the sites of covalent binding of acetate and malonate to the soluble pigeon liver fatty acid synthetase. Each of these compounds is bound to each of two peptide fractions which are released from the synthetase by pepsin digestion and then separated by Dowex ion-exchange chromatography. One of these peptide fractions has not been resolved. Further purification and study of the other peptide fraction has resulted in proof of the presence of 4′-phosphopantetheine bound through ester linkage to the peptide chain. In these experiments the peptides were labeled with either acetate-1- 14 C malonate-2- 14 C or pantothenic-1- 14 C acid. Quantitative analysis of the multi-enzyme complex for 4′-phosphopantetheine yielded a value close to 1 mole per mole of synthetase (450,000 gm). The implications of the findings that 1 mole of 4′-phosphopantetheine is found per mole of enzyme and that either acetate or malonate covalently bind to this compound are discussed.
- Subjects :
- Electrophoresis
Paper
Protein Hydrolysates
Biophysics
Peptide
Acetates
Biochemistry
Pantothenic Acid
Ligases
chemistry.chemical_compound
Mole
Animals
Binding site
Columbidae
Molecular Biology
chemistry.chemical_classification
Carbon Isotopes
Binding Sites
Fatty acid
Chromatography, Ion Exchange
Malonates
Pepsin A
Enzyme
Malonate
chemistry
Liver
Covalent bond
Ion Exchange Resins
Peptides
Quantitative analysis (chemistry)
Subjects
Details
- ISSN :
- 00039861
- Volume :
- 124
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Archives of biochemistry and biophysics
- Accession number :
- edsair.doi.dedup.....0fbdb86796510c9b97a3528ca99b0a31