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Abstract:

In this paper, cyclic adenosine-3′:5′-monophosphate-dependent protein kinase from yeast-like cells of Mucor rouxii is characterized. A scheme of partial purification is described together with Km for ATP (15 μm), histone (0.2 mg/ml), half-maximal activation constant for cyclic AMP (30 nm), and dissociation constant for the binding of cyclic AMP (40 nm). This enzyme is similar to type II protein kinases in two main aspects: the elution position in DEAE-cellulose chromatography and the readiness of its reassociation. But it has a singular characteristic: it does not dissociate completely with cyclic AMP alone (even at concentrations as high as 0.3 mm) unless histone or NaCl is present. NaCl displays several roles: helps dissociation, prevents inactivation of the catalytic subunit, inhibits enzyme activity, and does not prevent reassociation as occurs with type II protein kinases. Once the holoenzyme is dissociated, cyclic AMP is essential to maintain the enzyme in the dissociated state. © 1980.

Registro:

Documento: Artículo
Título:Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii
Autor:Moreno, S.; Passeron, S.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Buenos Aires, Cuidad Universitaria, 1428 Buenos Aires, Argentina
Palabras clave:cyclic amp; cyclic amp dependent protein kinase; animal experiment; fungus; in vitro study; mucor rouxii; Cyclic AMP; Dose-Response Relationship, Drug; Enzyme Activation; Histones; Macromolecular Systems; Mucor; Protein Kinases; Sodium Chloride; Substrate Specificity
Año:1980
Volumen:199
Número:2
Página de inicio:321
Página de fin:330
DOI: http://dx.doi.org/10.1016/0003-9861(80)90287-8
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:cyclic AMP, 60-92-4; Cyclic AMP, 60-92-4; Histones; Macromolecular Systems; Protein Kinases, EC 2.7.1.37; Sodium Chloride, 7647-14-5
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v199_n2_p321_Moreno

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Citas:

---------- APA ----------
Moreno, S. & Passeron, S. (1980) . Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii. Archives of Biochemistry and Biophysics, 199(2), 321-330.
http://dx.doi.org/10.1016/0003-9861(80)90287-8
---------- CHICAGO ----------
Moreno, S., Passeron, S. "Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii" . Archives of Biochemistry and Biophysics 199, no. 2 (1980) : 321-330.
http://dx.doi.org/10.1016/0003-9861(80)90287-8
---------- MLA ----------
Moreno, S., Passeron, S. "Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii" . Archives of Biochemistry and Biophysics, vol. 199, no. 2, 1980, pp. 321-330.
http://dx.doi.org/10.1016/0003-9861(80)90287-8
---------- VANCOUVER ----------
Moreno, S., Passeron, S. Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii. Arch. Biochem. Biophys. 1980;199(2):321-330.
http://dx.doi.org/10.1016/0003-9861(80)90287-8