Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii
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 disso...
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1980
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v199_n2_p321_Moreno http://hdl.handle.net/20.500.12110/paper_00039861_v199_n2_p321_Moreno |
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paper:paper_00039861_v199_n2_p321_Moreno2023-06-08T14:24:58Z Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii Moreno, Silvia N. J. 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 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. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1980 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v199_n2_p321_Moreno http://hdl.handle.net/20.500.12110/paper_00039861_v199_n2_p321_Moreno |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Moreno, Silvia N. J. Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii |
| topic_facet |
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 |
| description |
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. |
| author |
Moreno, Silvia N. J. |
| author_facet |
Moreno, Silvia N. J. |
| author_sort |
Moreno, Silvia N. J. |
| title |
Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii |
| title_short |
Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii |
| title_full |
Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii |
| title_fullStr |
Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii |
| title_full_unstemmed |
Further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus Mucor rouxii |
| title_sort |
further studies on cyclic adenosine 3′:5′-monophosphate protein kinase from dimorphic fungus mucor rouxii |
| publishDate |
1980 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v199_n2_p321_Moreno http://hdl.handle.net/20.500.12110/paper_00039861_v199_n2_p321_Moreno |
| work_keys_str_mv |
AT morenosilvianj furtherstudiesoncyclicadenosine35monophosphateproteinkinasefromdimorphicfungusmucorrouxii |
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