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Abstract:

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.

Registro:

Documento: Artículo
Título:Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes
Autor:Espinola, L.G.; Wider, E.A.; Stella, A.M.; Del C. Batlle, A.M.
Filiación:Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP, (CONICET and FCEN, University of Buenos Aires), Ciudad Universitaria, Pab. II, 1428 Buenos Aires, Argentina
Palabras clave:liposome; porphobilinogen synthase; biological model; blood and hemopoietic system; drug delivery system; drug efficacy; drug therapy; enzyme replacement; enzyme therapy; human; porphyria; therapy
Año:1983
Volumen:15
Número:3
Página de inicio:439
Página de fin:445
DOI: http://dx.doi.org/10.1016/0020-711X(83)90115-5
Título revista:International Journal of Biochemistry
Título revista abreviado:Int. J. Biochem.
ISSN:0020711X
CODEN:IJBOB
CAS:porphobilinogen synthase, 9036-37-7
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v15_n3_p439_Espinola

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Citas:

---------- APA ----------
Espinola, L.G., Wider, E.A., Stella, A.M. & Del C. Batlle, A.M. (1983) . Enzyme replacement therapy in porphyrias-II: Entrapment of δ-aminolaevulinate dehydratase in liposomes. International Journal of Biochemistry, 15(3), 439-445.
http://dx.doi.org/10.1016/0020-711X(83)90115-5
---------- CHICAGO ----------
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" . International Journal of Biochemistry 15, no. 3 (1983) : 439-445.
http://dx.doi.org/10.1016/0020-711X(83)90115-5
---------- MLA ----------
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" . International Journal of Biochemistry, vol. 15, no. 3, 1983, pp. 439-445.
http://dx.doi.org/10.1016/0020-711X(83)90115-5
---------- VANCOUVER ----------
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. Int. J. Biochem. 1983;15(3):439-445.
http://dx.doi.org/10.1016/0020-711X(83)90115-5