Protein kinase activities in Neurospora crassa
Several protein kinase activities have been found in 105,000g supernatant of Neurospora crassa mycelia grown up to the logarithmic phase. By chromatography on DEAE-cellulose the following enzyme activities have been resolved: (i) a cyclic AMP-dependent protein kinase (peak I kinase) eluting at 0.20...
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1981
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v206_n1_p87_Judewicz http://hdl.handle.net/20.500.12110/paper_00039861_v206_n1_p87_Judewicz |
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paper:paper_00039861_v206_n1_p87_Judewicz2023-06-08T14:24:59Z Protein kinase activities in Neurospora crassa Judewicz, Norberto D. Glikin, Gerardo Claudio Torres, Héctor Norberto cyclic AMP protamine kinase protein kinase article binding site enzymology ion exchange chromatography metabolism Neurospora Neurospora crassa Binding Sites Chromatography, DEAE-Cellulose Cyclic AMP Neurospora Neurospora crassa Protamine Kinase Protein Kinases Several protein kinase activities have been found in 105,000g supernatant of Neurospora crassa mycelia grown up to the logarithmic phase. By chromatography on DEAE-cellulose the following enzyme activities have been resolved: (i) a cyclic AMP-dependent protein kinase (peak I kinase) eluting at 0.20 m NaCl, more active with histone than with phosvitin (it was inhibited by both a thermolabile fraction having cyclic AMP-binding activity and a thermostable inhibitor isolated from 105,0005g mycelial supernates), (ii) a cyclic nucleotide-independent protein kinase (peak II kinase) eluting at 0.35 m NaCl, also more active with histone than with phosvitin (this kinase was not inhibited by the fraction having cyclic AMP-binding activity but it was sensitive to the thermostable inhibitor); and finally, (iii) a protein kinase eluting at 0.43 m NaCl (peak II kinase), with similar activity toward histone and phosvitin, insensitive to cyclic nucleotides and to fractions carrying cyclic AMP-binding capacity (this kinase activity also resulted insensitive to the thermostable inhibiting factor). © 1981. Fil:Judewicz, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Glikin, G.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1981 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v206_n1_p87_Judewicz http://hdl.handle.net/20.500.12110/paper_00039861_v206_n1_p87_Judewicz |
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 protamine kinase protein kinase article binding site enzymology ion exchange chromatography metabolism Neurospora Neurospora crassa Binding Sites Chromatography, DEAE-Cellulose Cyclic AMP Neurospora Neurospora crassa Protamine Kinase Protein Kinases |
spellingShingle |
cyclic AMP protamine kinase protein kinase article binding site enzymology ion exchange chromatography metabolism Neurospora Neurospora crassa Binding Sites Chromatography, DEAE-Cellulose Cyclic AMP Neurospora Neurospora crassa Protamine Kinase Protein Kinases Judewicz, Norberto D. Glikin, Gerardo Claudio Torres, Héctor Norberto Protein kinase activities in Neurospora crassa |
topic_facet |
cyclic AMP protamine kinase protein kinase article binding site enzymology ion exchange chromatography metabolism Neurospora Neurospora crassa Binding Sites Chromatography, DEAE-Cellulose Cyclic AMP Neurospora Neurospora crassa Protamine Kinase Protein Kinases |
description |
Several protein kinase activities have been found in 105,000g supernatant of Neurospora crassa mycelia grown up to the logarithmic phase. By chromatography on DEAE-cellulose the following enzyme activities have been resolved: (i) a cyclic AMP-dependent protein kinase (peak I kinase) eluting at 0.20 m NaCl, more active with histone than with phosvitin (it was inhibited by both a thermolabile fraction having cyclic AMP-binding activity and a thermostable inhibitor isolated from 105,0005g mycelial supernates), (ii) a cyclic nucleotide-independent protein kinase (peak II kinase) eluting at 0.35 m NaCl, also more active with histone than with phosvitin (this kinase was not inhibited by the fraction having cyclic AMP-binding activity but it was sensitive to the thermostable inhibitor); and finally, (iii) a protein kinase eluting at 0.43 m NaCl (peak II kinase), with similar activity toward histone and phosvitin, insensitive to cyclic nucleotides and to fractions carrying cyclic AMP-binding capacity (this kinase activity also resulted insensitive to the thermostable inhibiting factor). © 1981. |
author |
Judewicz, Norberto D. Glikin, Gerardo Claudio Torres, Héctor Norberto |
author_facet |
Judewicz, Norberto D. Glikin, Gerardo Claudio Torres, Héctor Norberto |
author_sort |
Judewicz, Norberto D. |
title |
Protein kinase activities in Neurospora crassa |
title_short |
Protein kinase activities in Neurospora crassa |
title_full |
Protein kinase activities in Neurospora crassa |
title_fullStr |
Protein kinase activities in Neurospora crassa |
title_full_unstemmed |
Protein kinase activities in Neurospora crassa |
title_sort |
protein kinase activities in neurospora crassa |
publishDate |
1981 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v206_n1_p87_Judewicz http://hdl.handle.net/20.500.12110/paper_00039861_v206_n1_p87_Judewicz |
work_keys_str_mv |
AT judewicznorbertod proteinkinaseactivitiesinneurosporacrassa AT glikingerardoclaudio proteinkinaseactivitiesinneurosporacrassa AT torreshectornorberto proteinkinaseactivitiesinneurosporacrassa |
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1768544756345864192 |