dc.creatorRimoldi, Omar Jorge
dc.creatorSoulages, José L.
dc.creatorGonzález, S. M.
dc.creatorPeluffo, R. O.
dc.creatorBrenner, Rodolfo Roberto
dc.date1989
dc.date2021-06-17T13:04:45Z
dc.date.accessioned2023-07-15T02:08:20Z
dc.date.available2023-07-15T02:08:20Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/120429
dc.identifierissn:0022-2275
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7460830
dc.descriptionThe very high density lipoprotein (VHDL) of Triatoma injesfum hemolymph from adult males has been isolated and purified by two-step density gradient ultracentrifugation. It appears to be homogeneous as judged by native polyacrylamide gel electrophoresis. The content of VHDL in hemolymph was estimated to be 8 mg proteidml. The purified protein has a molecular weight (M,) of 450,000, is composed of six subunits of M, p 77,000, and possesses a high content of aromatic amino acids. This protein is glycosylated and contains 3% of lipids by weight with a remarkable amount of free fatty acids (25% of total lipids). The I: injesfans VHDL has a different lipid and amino acid composition from lipophorin. The lipid composition and the spectroscopic studies using cis-parinaric acid indicated a high fatty acid binding affinity. It has nine binding sites per mol of VHDL. Competence studies revealed that VHDL has its highest affinity for the binding of palmitic acid followed by stearic and arachidonic acids.
dc.descriptionInstituto de Investigaciones Bioquímicas de La Plata
dc.formatapplication/pdf
dc.format857-864
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by/4.0/
dc.rightsCreative Commons Attribution 4.0 International (CC BY 4.0)
dc.subjectBiología
dc.subjectInsect lipoproteins
dc.subjectFree fatty acid trasnport
dc.subjectInsect VHDL
dc.subjectLipid-protein interactions
dc.titlePurification and properties of the very high density lipoprotein from the hemolymph of adult Triatoma infestans
dc.typeArticulo
dc.typeArticulo


Este ítem pertenece a la siguiente institución