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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Autores principales: Judewicz, Norberto D., Glikin, Gerardo Claudio, Torres, Héctor Norberto
Publicado: 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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spelling 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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