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Preliminary characterization of the delta-9 desaturase of Tetrahymena pyriformis W.
Metadata
JournalComp. Biochem. Physiol., BNot FoundDate
1978
Type
Research Support, U.S. Gov't, P.H.S.
Research Support, Non-U.S. Gov't
Journal Article
Volume
1978 / 61 : 513-20
Author
Shipiro H 1, Prescott D , Rabinowitz JL
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Doi
PMIDMESH
Animals
Fatty Acid Desaturases
Stearoyl-CoA Desaturase
Substrate Specificity
Temperature
Tetrahymena pyriformis
Abstract
1. In vitro assay conditions have been defined for measurement of delta 9 desaturase activity in Tetrahymena pyriformis W. 2. The reaction depends on the presence of oxygen and a reduced pyridine nucleotide cofactor. FAD supports a low level of enzymatic activity. 3. Both stearyl-CoA and palmityl-CoA are acceptable substrates. Oleate formation is maximal at 30 degrees C. 4. Delta-9 desaturase activity appears to be localized in the microsomal fraction. Delta-6 and/or delta 12 desaturase activities have also been observed. 5. When the specificity of the delta 9 desaturase towards stearyl-CoA and palmityl-CoA was observed at 30 and 16 degrees C it was found that lowering the assay temperature did not affect specificity. Stearyl-CoA was more readily desaturated at both temperatures. 6. Exogenous oleyl-CoA and diisopropylfluorophosphate had little effect on delta 9 desaturase activity. However, cyanide strongly inhibited desaturation and a sensitivity to sulfhydryl-binding reagents has also been demonstrated.
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Comp. Biochem. Physiol., BComparative biochemistry and physiology. B, Comparative biochemistry
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