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Abstract:

Bovine liver aminolaevulate dehydratase (ALAD) has been chemically attached to Sepharose 4B and its properties have been studied. The optimal conditions for coupling have been determined. It was found that the immobilized enzyme retained a significant percentage of the activity of the free enzyme. The coupling yield was rather high. The insolubilized enzyme requires both anaerobiosis and a thiol activator for maximal activity. It can be stored at 4 °C for long periods with little loss of activity and it can be repeatedly used without alteration of its enzymic capacity. Attachment of ALA-D to the gel has led to an enhanced thermal stability. pH optima of free and bound enzyme was the same while a small decrease in the Km of the matrix bonded ALA-D as compared to that of the soluble enzyme was observed. The use of the fixed-ALA-D for the preparation of PBG is described. © 1977 Dr. W. Junk b.v. Publishers.

Registro:

Documento: Artículo
Título:Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose
Autor:Stella, A.M.; de Xifra, E.W.; Batlle, A.M.d.C.
Filiación:Laboratorio de Porfirinas, Departamento de Quimica Biologica, Facultad de Ciencia Exactas y Naturales, Universidad de Buenos Aires, Argentina
Palabras clave:enzyme; liver enzyme; porphobilinogen synthase; porphyrin; cattle; in vitro study; theoretical study; Animal; Cattle; Comparative Study; Drug Stability; Enzymes, Immobilized; Hydro-Lyases; Hydrogen-Ion Concentration; Kinetics; Liver; Methods; Porphobilinogen; Porphobilinogen Synthase; Sepharose; Temperature
Año:1977
Volumen:16
Número:2-3
Página de inicio:97
Página de fin:104
DOI: http://dx.doi.org/10.1007/BF01732049
Título revista:Molecular and Cellular Biochemistry
Título revista abreviado:Mol Cell Biochem
ISSN:03008177
CODEN:MCBIB
CAS:porphobilinogen synthase, 9036-37-7; porphyrin, 24869-67-8; Enzymes, Immobilized; Hydro-Lyases, EC 4.2.1.; Porphobilinogen Synthase, EC 4.2.1.24; Porphobilinogen, 487-90-1; Sepharose, 9012-36-6
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p97_Stella

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Citas:

---------- APA ----------
Stella, A.M., de Xifra, E.W. & Batlle, A.M.d.C. (1977) . Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose. Molecular and Cellular Biochemistry, 16(2-3), 97-104.
http://dx.doi.org/10.1007/BF01732049
---------- CHICAGO ----------
Stella, A.M., de Xifra, E.W., Batlle, A.M.d.C. "Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose" . Molecular and Cellular Biochemistry 16, no. 2-3 (1977) : 97-104.
http://dx.doi.org/10.1007/BF01732049
---------- MLA ----------
Stella, A.M., de Xifra, E.W., Batlle, A.M.d.C. "Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose" . Molecular and Cellular Biochemistry, vol. 16, no. 2-3, 1977, pp. 97-104.
http://dx.doi.org/10.1007/BF01732049
---------- VANCOUVER ----------
Stella, A.M., de Xifra, E.W., Batlle, A.M.d.C. Porphyrin biosynthesis. Immobilized enzymes IV. Studies on aminolaevulate dehydratase attached to Sepharose. Mol Cell Biochem. 1977;16(2-3):97-104.
http://dx.doi.org/10.1007/BF01732049