Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.

Autores
Catalá, Ángel
Año de publicación
1993
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This paper reviews characteristics of microsomal membrane structure; long chain fatty acids, acyl CoA derivatives, retinoids and the microsomal formation of acyl CoA derivatives and retinyl esters. It is analyzed how the movement of these molecules at the intracellular level is affected by their respective binding proteins (Fatty acid binding protein, acyl CoA binding protein and cellular retinol binding protein). Studies with model systems using these hydrophobic ligands and the lipid-binding or transfer proteins are also described. This topic is of interest especially because in the esterification of retinol the three substrates and the three binding proteins may interact.
Facultad de Ciencias Veterinarias
Materia
Bioquímica
Fatty acid binding protein
Microsomes
Long chain fatty acids
Acyl-CoA derivatives
Retinoids, liver
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/144027
Acceder
id SEDICI_f8a198033a3db5173487f9e5360c5894
oai_identifier_str oai:sedici.unlp.edu.ar:10915/144027
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.Catalá, ÁngelBioquímicaFatty acid binding proteinMicrosomesLong chain fatty acidsAcyl-CoA derivativesRetinoids, liverThis paper reviews characteristics of microsomal membrane structure; long chain fatty acids, acyl CoA derivatives, retinoids and the microsomal formation of acyl CoA derivatives and retinyl esters. It is analyzed how the movement of these molecules at the intracellular level is affected by their respective binding proteins (Fatty acid binding protein, acyl CoA binding protein and cellular retinol binding protein). Studies with model systems using these hydrophobic ligands and the lipid-binding or transfer proteins are also described. This topic is of interest especially because in the esterification of retinol the three substrates and the three binding proteins may interact.Facultad de Ciencias Veterinarias1993-03-24info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf89-94http://sedici.unlp.edu.ar/handle/10915/144027enginfo:eu-repo/semantics/altIdentifier/issn/0300-8177info:eu-repo/semantics/altIdentifier/issn/1573-4919info:eu-repo/semantics/altIdentifier/doi/10.1007/bf00926080info:eu-repo/semantics/altIdentifier/pmid/8387630info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:31Zoai:sedici.unlp.edu.ar:10915/144027Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:32.058SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
title Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
spellingShingle Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
Catalá, Ángel
Bioquímica
Fatty acid binding protein
Microsomes
Long chain fatty acids
Acyl-CoA derivatives
Retinoids, liver
title_short Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
title_full Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
title_fullStr Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
title_full_unstemmed Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
title_sort Interaction of fatty acids, acyl-CoA derivatives and retinoids with microsomal membranes: effect of cytosolic proteins.
dc.creator.none.fl_str_mv Catalá, Ángel
author Catalá, Ángel
author_facet Catalá, Ángel
author_role author
dc.subject.none.fl_str_mv Bioquímica
Fatty acid binding protein
Microsomes
Long chain fatty acids
Acyl-CoA derivatives
Retinoids, liver
topic Bioquímica
Fatty acid binding protein
Microsomes
Long chain fatty acids
Acyl-CoA derivatives
Retinoids, liver
dc.description.none.fl_txt_mv This paper reviews characteristics of microsomal membrane structure; long chain fatty acids, acyl CoA derivatives, retinoids and the microsomal formation of acyl CoA derivatives and retinyl esters. It is analyzed how the movement of these molecules at the intracellular level is affected by their respective binding proteins (Fatty acid binding protein, acyl CoA binding protein and cellular retinol binding protein). Studies with model systems using these hydrophobic ligands and the lipid-binding or transfer proteins are also described. This topic is of interest especially because in the esterification of retinol the three substrates and the three binding proteins may interact.
Facultad de Ciencias Veterinarias
description This paper reviews characteristics of microsomal membrane structure; long chain fatty acids, acyl CoA derivatives, retinoids and the microsomal formation of acyl CoA derivatives and retinyl esters. It is analyzed how the movement of these molecules at the intracellular level is affected by their respective binding proteins (Fatty acid binding protein, acyl CoA binding protein and cellular retinol binding protein). Studies with model systems using these hydrophobic ligands and the lipid-binding or transfer proteins are also described. This topic is of interest especially because in the esterification of retinol the three substrates and the three binding proteins may interact.
publishDate 1993
dc.date.none.fl_str_mv 1993-03-24
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/144027
url http://sedici.unlp.edu.ar/handle/10915/144027
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0300-8177
info:eu-repo/semantics/altIdentifier/issn/1573-4919
info:eu-repo/semantics/altIdentifier/doi/10.1007/bf00926080
info:eu-repo/semantics/altIdentifier/pmid/8387630
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
89-94
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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