Abstract
The structural properties of purified palmitoyl-CoA synthetase from rat liver microsomal material were investigated. The active enzyme has a molecular weight of 168000 and contains about 8.2mol of phospholipid bound/mol of enzyme protein, as well as bound fatty acids. Association of the active enzyme was shown to occur, without impairment of catalytic activity. The lowest-molecular-weight species obtained under denaturing conditions was 27000 daltons.
MeSH terms
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Amino Acids / analysis
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Animals
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Chemical Phenomena
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Chemistry
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Chromatography, Gel
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Coenzyme A Ligases* / analysis
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Electrophoresis, Polyacrylamide Gel
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Isoelectric Focusing
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Lipids / analysis
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Macromolecular Substances
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Microsomes, Liver / enzymology*
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Molecular Weight
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Palmitic Acids
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Phospholipids / analysis
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Protein Binding
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Protein Denaturation
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Rats
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Sodium Dodecyl Sulfate
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Tritium
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Ultracentrifugation
Substances
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Amino Acids
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Lipids
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Macromolecular Substances
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Palmitic Acids
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Phospholipids
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Tritium
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Sodium Dodecyl Sulfate
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Coenzyme A Ligases