Hydrophobic nature of rat lymph chylomicrons

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dc.authoridbay karabulut, aysun/0000-0002-7873-2805
dc.authorwosidGüldür, Tayfun/AAA-7088-2021
dc.authorwosidbay karabulut, aysun/HJP-0995-2023
dc.contributor.authorGüldür, T
dc.contributor.authorKarabulut, AB
dc.contributor.authorBayraktar, N
dc.contributor.authorKaynar, Ö
dc.date.accessioned2024-08-04T20:13:47Z
dc.date.available2024-08-04T20:13:47Z
dc.date.issued2004
dc.departmentİnönü Üniversitesien_US
dc.description.abstractBackground: A typical molecular structure of a lipoprotein is composed of hydrophobic lipids at the core and hydrophilic apolipoprotein side chains and lipid head groups at the surface. Some of the hydrophobic characteristics of rat lymph chylomicrons were investigated. Methods: Thoracic duct was cannulated and lymph was collected overnight. Chylomicrons (>100 rim) were isolated by ultracentrifugation at 4 x 10(6) x g min. Since particle aggregation is a characteristic of hydrophobic nature of lipoproteins, as an index of aggregation, the turbidity generated by vortexing and storage of chylomicrons was measured spectrophotometrically at 680 nm. We also assessed the ability of chylomicrons to interact with five different hydrophobic interaction chromatography (HIC) media. Results: Neither shaking nor prolonged storage at 4 degreesC produced an increase in the optical density of chylomicron solution indicating no aggregation took place. Typical elution profiles of chylomicrons through octyl, phenyl (high substance) and butyl sepharose columns showed two peaks. Peak I material emerged with 4 mol/l NaCl in a position corresponding to the void volume and peak II material eluted with water. Phenyl sepharose (high performance) media exhibited the maximum binding strength towards chylomicrons among the five different media. In the case of pheryl sepharose (low substance) column, an additional material was eluted with 3 mol/l NaCl between peaks I and II. These results indicate the heterogeneity of chylomicron surface hydrophobicity. Conclusion: Since particle aggregation is a characteristics of hydrophobicity of lipoproteins and believed to be an underlying cause of atherosclerosis, fractionation of lipoproteins by hydrophobic interaction chromatography may introduce a new approach into the assessment of lipoprotein atherogeneicity. (C) 2004 Elsevier B.V. All rights reserved.en_US
dc.identifier.doi10.1016/j.cccn.2003.12.018
dc.identifier.endpage169en_US
dc.identifier.issn0009-8981
dc.identifier.issn1873-3492
dc.identifier.issue1-2en_US
dc.identifier.pmid15026277en_US
dc.identifier.scopus2-s2.0-1542499817en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage161en_US
dc.identifier.urihttps://doi.org/10.1016/j.cccn.2003.12.018
dc.identifier.urihttps://hdl.handle.net/11616/93849
dc.identifier.volume342en_US
dc.identifier.wosWOS:000220526400016en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofClinica Chimica Actaen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectaggregationen_US
dc.subjectchylomicronen_US
dc.subjecthydrophobicityen_US
dc.subjectatherosclerosisen_US
dc.subjectchromatographyen_US
dc.titleHydrophobic nature of rat lymph chylomicronsen_US
dc.typeArticleen_US

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