The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii

Soluble preparations from mycelium of the dimorphic fungus Mucor rouxii contained detectable amounts of phosphoprotein phosphatase activity. This cytosolic phosphatase activity exhibited a molecular weight below 80,000 and could be resolved into two different forms (enzymes I and II) by chromatograp...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autor principal:	Seigelchifer, Mauricio Angel
Publicado:	1984
Materias:	manganese phosphoprotein phosphatase article cytosol enzyme specificity enzymology isolation and purification kinetics metabolism molecular weight Mucor Cytosol Kinetics Manganese Molecular Weight Phosphoprotein Phosphatase Substrate Specificity Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v229_n1_p403_Seigelchifer http://hdl.handle.net/20.500.12110/paper_00039861_v229_n1_p403_Seigelchifer
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00039861_v229_n1_p403_Seigelchifer
record_format	dspace
spelling	paper:paper_00039861_v229_n1_p403_Seigelchifer2023-06-08T14:25:01Z The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii Seigelchifer, Mauricio Angel manganese phosphoprotein phosphatase article cytosol enzyme specificity enzymology isolation and purification kinetics metabolism molecular weight Mucor Cytosol Kinetics Manganese Molecular Weight Mucor Phosphoprotein Phosphatase Substrate Specificity Support, Non-U.S. Gov't Soluble preparations from mycelium of the dimorphic fungus Mucor rouxii contained detectable amounts of phosphoprotein phosphatase activity. This cytosolic phosphatase activity exhibited a molecular weight below 80,000 and could be resolved into two different forms (enzymes I and II) by chromatography on DEAE-cellulose followed by gel filtration on Sephacryl S-300. Enzyme I (Mr 64,000) was mainly a histone phosphatase activity, absolutely dependent on divalent cations, with a K0.5 for MnCl2 of 2 mm. Enzyme II (Mr 40,000) was active with histone and phosphorylase. Its activity was independent or slightly inhibited by Mn2+. This enzyme was strongly inhibited by 50 mm NaF or 1 mm ATP. When partially purified enzymes I and II were separately treated with ethanol, the catalytic properties of enzyme II were apparently not affected while those of enzyme I were drastically changed. The activity with histone, which was originally dependent on Mn2+, became independent or slightly inhibited by the cation. The treatment was accompanied by a notable increase in phosphorylase phosphatase activity which was strongly inhibited by Mn2+. Treated enzyme I eluted from DEAE-cellulose and Sephacryl S-300 columns at a position similar to that of enzyme II. © 1984. Fil:Seigelchifer, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1984 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v229_n1_p403_Seigelchifer http://hdl.handle.net/20.500.12110/paper_00039861_v229_n1_p403_Seigelchifer
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	manganese phosphoprotein phosphatase article cytosol enzyme specificity enzymology isolation and purification kinetics metabolism molecular weight Mucor Cytosol Kinetics Manganese Molecular Weight Mucor Phosphoprotein Phosphatase Substrate Specificity Support, Non-U.S. Gov't
spellingShingle	manganese phosphoprotein phosphatase article cytosol enzyme specificity enzymology isolation and purification kinetics metabolism molecular weight Mucor Cytosol Kinetics Manganese Molecular Weight Mucor Phosphoprotein Phosphatase Substrate Specificity Support, Non-U.S. Gov't Seigelchifer, Mauricio Angel The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
topic_facet	manganese phosphoprotein phosphatase article cytosol enzyme specificity enzymology isolation and purification kinetics metabolism molecular weight Mucor Cytosol Kinetics Manganese Molecular Weight Mucor Phosphoprotein Phosphatase Substrate Specificity Support, Non-U.S. Gov't
description	Soluble preparations from mycelium of the dimorphic fungus Mucor rouxii contained detectable amounts of phosphoprotein phosphatase activity. This cytosolic phosphatase activity exhibited a molecular weight below 80,000 and could be resolved into two different forms (enzymes I and II) by chromatography on DEAE-cellulose followed by gel filtration on Sephacryl S-300. Enzyme I (Mr 64,000) was mainly a histone phosphatase activity, absolutely dependent on divalent cations, with a K0.5 for MnCl2 of 2 mm. Enzyme II (Mr 40,000) was active with histone and phosphorylase. Its activity was independent or slightly inhibited by Mn2+. This enzyme was strongly inhibited by 50 mm NaF or 1 mm ATP. When partially purified enzymes I and II were separately treated with ethanol, the catalytic properties of enzyme II were apparently not affected while those of enzyme I were drastically changed. The activity with histone, which was originally dependent on Mn2+, became independent or slightly inhibited by the cation. The treatment was accompanied by a notable increase in phosphorylase phosphatase activity which was strongly inhibited by Mn2+. Treated enzyme I eluted from DEAE-cellulose and Sephacryl S-300 columns at a position similar to that of enzyme II. © 1984.
author	Seigelchifer, Mauricio Angel
author_facet	Seigelchifer, Mauricio Angel
author_sort	Seigelchifer, Mauricio Angel
title	The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
title_short	The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
title_full	The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
title_fullStr	The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
title_full_unstemmed	The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
title_sort	separation and properties of two phosphoprotein phosphatases from the dimorphic fungus mucor rouxii
publishDate	1984
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v229_n1_p403_Seigelchifer http://hdl.handle.net/20.500.12110/paper_00039861_v229_n1_p403_Seigelchifer
work_keys_str_mv	AT seigelchifermauricioangel theseparationandpropertiesoftwophosphoproteinphosphatasesfromthedimorphicfungusmucorrouxii AT seigelchifermauricioangel separationandpropertiesoftwophosphoproteinphosphatasesfromthedimorphicfungusmucorrouxii
_version_	1768542013012049920

The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii

Ejemplares similares