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Abstract:

Soluble nucleoside-diphosphate kinase (NDP kinase) fromCandida albicanswas purified to electrophoretic homogeneity and a partial sequence was determined. The enzyme was kinetically and physically characterized. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed a single polypeptide of 17 kDa upon staining, by immunodetection with heterologous and homologous antibodies, and by autoradiography of the phosphorylated enzyme. Furthermore, isoelectric focusing of the purified native enzyme showed a single acidic band (pI4.5). These results together with a native molecular mass of 98 kDa suggest a hexameric native enzyme composed of identical subunits. Like NDP kinases from other sources, the catalysis involves a phosphoenzyme intermediate that is rapidly formed upon incubation of the enzyme with ATP. The transfer of phosphate from phosphoprotein intermediate to nucleoside diphosphates is equally fast. Kinetic experiments indicated that GTP and ATP had the lowestKmcompared to UTP, dTTP, and CTP. GDP acted as a preferred acceptor as assessed by kinetic measurements as well as by competition experiments. Experimental data are presented indicating the existence of a membrane-associated NDP kinase. Preliminary characterization of this enzyme suggests that cytosolic and membrane-associated NDP kinases are similar proteins. © 1995 Academic Press, Inc.

Registro:

Documento: Artículo
Título:Candida albicans nucleoside-diphosphate kinase: Purification and characterization
Autor:Biondi, R.M.; Veron, M.; Walz, K.; Passeron, S.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellópn II, Ciudad Universitaria, 1428, 1428 Buenos Aires, Argentina
Unité de Biochimie Cellulaire, CNRS, URA 1129, Institut Pasteur, 75724 Paris Cedex 15, France
Cátedra de Microbiología, Facultad de Agronomía, Universidad de Buenos Aires, Avda. San Martín 4453, 1417 Buenos Aires, Argentina
Palabras clave:adenosine triphosphate; antibody; cytidine triphosphate; guanosine diphosphate; guanosine triphosphate; nucleoside diphosphate kinase; phosphate; phosphoprotein; polypeptide; thymidine triphosphate; uridine triphosphate; article; autoradiography; candida albicans; catalysis; enzyme activity; enzyme purification; isoelectric focusing; nonhuman; polyacrylamide gel electrophoresis; priority journal; thin layer chromatography; Amino Acid Sequence; Candida albicans; Kinetics; Molecular Sequence Data; Nucleoside-Diphosphate Kinase; Phosphorylation; Sequence Alignment; Support, Non-U.S. Gov't; Candida albicans
Año:1995
Volumen:323
Número:1
Página de inicio:187
Página de fin:194
DOI: http://dx.doi.org/10.1006/abbi.1995.0025
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CAS:Nucleoside-Diphosphate Kinase, EC 2.7.4.6
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v323_n1_p187_Biondi

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Citas:

---------- APA ----------
Biondi, R.M., Veron, M., Walz, K. & Passeron, S. (1995) . Candida albicans nucleoside-diphosphate kinase: Purification and characterization. Archives of Biochemistry and Biophysics, 323(1), 187-194.
http://dx.doi.org/10.1006/abbi.1995.0025
---------- CHICAGO ----------
Biondi, R.M., Veron, M., Walz, K., Passeron, S. "Candida albicans nucleoside-diphosphate kinase: Purification and characterization" . Archives of Biochemistry and Biophysics 323, no. 1 (1995) : 187-194.
http://dx.doi.org/10.1006/abbi.1995.0025
---------- MLA ----------
Biondi, R.M., Veron, M., Walz, K., Passeron, S. "Candida albicans nucleoside-diphosphate kinase: Purification and characterization" . Archives of Biochemistry and Biophysics, vol. 323, no. 1, 1995, pp. 187-194.
http://dx.doi.org/10.1006/abbi.1995.0025
---------- VANCOUVER ----------
Biondi, R.M., Veron, M., Walz, K., Passeron, S. Candida albicans nucleoside-diphosphate kinase: Purification and characterization. Arch. Biochem. Biophys. 1995;323(1):187-194.
http://dx.doi.org/10.1006/abbi.1995.0025