dc.creatorLeikin, Alicia Isabel
dc.creatorNervi, Aníbal M.
dc.creatorBrenner, Rodolfo Roberto
dc.date1979
dc.date2022-06-08T13:27:33Z
dc.date.accessioned2023-07-15T05:00:33Z
dc.date.available2023-07-15T05:00:33Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/137522
dc.identifierissn:0024-4201
dc.identifierissn:1558-9307
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7471735
dc.descriptionSuspension and centrifugation of crude microsomes of rat liver in low ionic strength solution separated a soluble protein fraction that is necessary for the full activity of the linoleic acid desaturase. The fraction partially purified through Sephadex G-150 still retains lipids which are mainly constituted by phosphatidylcholine. Linoleic acid predominates in the fatty acid composition. By NaCl gradient centrifugation and electrophoresis in gelatinized cellulose acetate, the factor behaves like a lipoprotein. The factor binds linoleic acid and linolyl-CoA that are desaturated to γ-linolenic acid when incubated with washed microsomes. Albumin does not replace the factor.
dc.descriptionFacultad de Ciencias Médicas
dc.formatapplication/pdf
dc.format1021-1026
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.subjectBioquímica
dc.subjectLipid
dc.subjectLinoleic acid
dc.titleLipid binding properties of a factor necessary for linoleic acid desaturation
dc.typeArticulo
dc.typeArticulo


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