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, N.D., Glikin, G.C., Torres, H.N.
Formato:	JOUR
Materias:	cyclic AMP protamine kinase protein kinase article binding site enzymology ion exchange chromatography metabolism Neurospora Neurospora crassa Binding Sites Chromatography, DEAE-Cellulose Cyclic AMP Protamine Kinase Protein Kinases
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00039861_v206_n1_p87_Judewicz
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00039861_v206_n1_p87_Judewicz
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spelling	todo:paper_00039861_v206_n1_p87_Judewicz2023-10-03T13:56:55Z Protein kinase activities in Neurospora crassa Judewicz, N.D. Glikin, G.C. Torres, H.N. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, N.D. Glikin, G.C. Torres, H.N. 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.
format	JOUR
author	Judewicz, N.D. Glikin, G.C. Torres, H.N.
author_facet	Judewicz, N.D. Glikin, G.C. Torres, H.N.
author_sort	Judewicz, N.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
url	http://hdl.handle.net/20.500.12110/paper_00039861_v206_n1_p87_Judewicz
work_keys_str_mv	AT judewicznd proteinkinaseactivitiesinneurosporacrassa AT glikingc proteinkinaseactivitiesinneurosporacrassa AT torreshn proteinkinaseactivitiesinneurosporacrassa
_version_	1807317682330009600

Protein kinase activities in Neurospora crassa

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