Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes

1. 1. Different types of neutral and negative, large, small and multilamellar liposomes were prepared and conditions for entrapping partially and highly purified preparations of blood and bovine ALA-dehydratase were studied. 2. 2. Gel filtration on Sepharose 4B, resolved liposomes formed in the abse...

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Autores principales: Espinola, L.G., Wider, E.A., Stella, A.M., Del C. Batlle, A.M.
Formato: JOUR
Materias:
liposome
porphobilinogen synthase
biological model
blood and hemopoietic system
drug delivery system
drug efficacy
drug therapy
enzyme replacement
enzyme therapy
human
porphyria
therapy
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v15_n3_p439_Espinola
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_0020711X_v15_n3_p439_Espinola2023-10-03T14:17:47Z Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes Espinola, L.G. Wider, E.A. Stella, A.M. Del C. Batlle, A.M. liposome porphobilinogen synthase biological model blood and hemopoietic system drug delivery system drug efficacy drug therapy enzyme replacement enzyme therapy human porphyria therapy 1. 1. Different types of neutral and negative, large, small and multilamellar liposomes were prepared and conditions for entrapping partially and highly purified preparations of blood and bovine ALA-dehydratase were studied. 2. 2. Gel filtration on Sepharose 4B, resolved liposomes formed in the absence of enzyme from free enzyme, when both were chromatographed 1-2 hr after mixing, showing that ALA-D did not become associated with liposomes. 3. 3. Preparation of liposomes in the presence of ALA-D resulted in partial entrapment of the enzyme and separation of the protein-containing liposomes from excess free protein was achieved by Sepharose 4B gel filtration. 4. 4. Part of the activity of ALA-D associated with liposomes was latent, and it could only be detected after treatment with Triton X-100, which, at the concentration used, disrupted the spherules and did not affect ALA-D activity. Some activity was also measured in intact ALA-D loaded liposomes. 5. 5. Of all preparations of liposomes, best entrapment values for ALA-D were consistently obtained with negatively charged large multilamellar vesicles, (-LMV (ALA-D)). Considerable less yield was associated with negative small unilamellar vesicles (-SUV) and neutral large unilamellar vesicles (nLUV). © 1983. Fil:Espinola, L.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v15_n3_p439_Espinola
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic liposome
porphobilinogen synthase
biological model
blood and hemopoietic system
drug delivery system
drug efficacy
drug therapy
enzyme replacement
enzyme therapy
human
porphyria
therapy
spellingShingle liposome
porphobilinogen synthase
biological model
blood and hemopoietic system
drug delivery system
drug efficacy
drug therapy
enzyme replacement
enzyme therapy
human
porphyria
therapy
Espinola, L.G.
Wider, E.A.
Stella, A.M.
Del C. Batlle, A.M.
Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
topic_facet liposome
porphobilinogen synthase
biological model
blood and hemopoietic system
drug delivery system
drug efficacy
drug therapy
enzyme replacement
enzyme therapy
human
porphyria
therapy
description 1. 1. Different types of neutral and negative, large, small and multilamellar liposomes were prepared and conditions for entrapping partially and highly purified preparations of blood and bovine ALA-dehydratase were studied. 2. 2. Gel filtration on Sepharose 4B, resolved liposomes formed in the absence of enzyme from free enzyme, when both were chromatographed 1-2 hr after mixing, showing that ALA-D did not become associated with liposomes. 3. 3. Preparation of liposomes in the presence of ALA-D resulted in partial entrapment of the enzyme and separation of the protein-containing liposomes from excess free protein was achieved by Sepharose 4B gel filtration. 4. 4. Part of the activity of ALA-D associated with liposomes was latent, and it could only be detected after treatment with Triton X-100, which, at the concentration used, disrupted the spherules and did not affect ALA-D activity. Some activity was also measured in intact ALA-D loaded liposomes. 5. 5. Of all preparations of liposomes, best entrapment values for ALA-D were consistently obtained with negatively charged large multilamellar vesicles, (-LMV (ALA-D)). Considerable less yield was associated with negative small unilamellar vesicles (-SUV) and neutral large unilamellar vesicles (nLUV). © 1983.
format JOUR
author Espinola, L.G.
Wider, E.A.
Stella, A.M.
Del C. Batlle, A.M.
author_facet Espinola, L.G.
Wider, E.A.
Stella, A.M.
Del C. Batlle, A.M.
author_sort Espinola, L.G.
title Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
title_short Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
title_full Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
title_fullStr Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
title_full_unstemmed Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
title_sort enzyme replacement therapy in porphyrias-ii: entrapment of δ-aminolaevulinate dehydratase in liposomes
url http://hdl.handle.net/20.500.12110/paper_0020711X_v15_n3_p439_Espinola
work_keys_str_mv AT espinolalg enzymereplacementtherapyinporphyriasiientrapmentofdaminolaevulinatedehydrataseinliposomes
AT widerea enzymereplacementtherapyinporphyriasiientrapmentofdaminolaevulinatedehydrataseinliposomes
AT stellaam enzymereplacementtherapyinporphyriasiientrapmentofdaminolaevulinatedehydrataseinliposomes
AT delcbatlleam enzymereplacementtherapyinporphyriasiientrapmentofdaminolaevulinatedehydrataseinliposomes
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