The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii

Two heat-stable inhibitors (a and b) of phosphoprotein phosphatases I and II from Mucor rouxii were isolated from mycelium of the fungus. They were partially purified from extracts by heating, DEAE-cellulose chromatography, and Sephadex G-75 gel filtration. The molecular weights of inhibitors a and...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autor principal:	Seigelchifer, Mauricio Angel
Publicado:	1985
Materias:	enzyme inhibitor phosphatase phosphoprotein fungus mucor rouxii nonhuman priority journal protein phosphorylation Chemistry Chromatography, Gel Heat Molecular Weight Mucor Phosphoprotein Phosphatase Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v238_n1_p353_Seigelchifer http://hdl.handle.net/20.500.12110/paper_00039861_v238_n1_p353_Seigelchifer
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00039861_v238_n1_p353_Seigelchifer
record_format	dspace
spelling	paper:paper_00039861_v238_n1_p353_Seigelchifer2023-06-08T14:25:01Z The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii Seigelchifer, Mauricio Angel enzyme inhibitor phosphatase phosphoprotein fungus mucor rouxii nonhuman priority journal protein phosphorylation Chemistry Chromatography, Gel Heat Molecular Weight Mucor Phosphoprotein Phosphatase Support, Non-U.S. Gov't Two heat-stable inhibitors (a and b) of phosphoprotein phosphatases I and II from Mucor rouxii were isolated from mycelium of the fungus. They were partially purified from extracts by heating, DEAE-cellulose chromatography, and Sephadex G-75 gel filtration. The molecular weights of inhibitors a and b, estimated by gel filtration, are 5,000 and 20,000 respectively. Inhibitor a acts similarly on both enzymes while inhibitor b is relatively more active on enzyme II. Storage of inhibitor b at -20 °C for several weeks resulted in a partial conversion to a lower-molecular-weight form with properties similar to those of inhibitor a. © 1985. Fil:Seigelchifer, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1985 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v238_n1_p353_Seigelchifer http://hdl.handle.net/20.500.12110/paper_00039861_v238_n1_p353_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	enzyme inhibitor phosphatase phosphoprotein fungus mucor rouxii nonhuman priority journal protein phosphorylation Chemistry Chromatography, Gel Heat Molecular Weight Mucor Phosphoprotein Phosphatase Support, Non-U.S. Gov't
spellingShingle	enzyme inhibitor phosphatase phosphoprotein fungus mucor rouxii nonhuman priority journal protein phosphorylation Chemistry Chromatography, Gel Heat Molecular Weight Mucor Phosphoprotein Phosphatase Support, Non-U.S. Gov't Seigelchifer, Mauricio Angel The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii
topic_facet	enzyme inhibitor phosphatase phosphoprotein fungus mucor rouxii nonhuman priority journal protein phosphorylation Chemistry Chromatography, Gel Heat Molecular Weight Mucor Phosphoprotein Phosphatase Support, Non-U.S. Gov't
description	Two heat-stable inhibitors (a and b) of phosphoprotein phosphatases I and II from Mucor rouxii were isolated from mycelium of the fungus. They were partially purified from extracts by heating, DEAE-cellulose chromatography, and Sephadex G-75 gel filtration. The molecular weights of inhibitors a and b, estimated by gel filtration, are 5,000 and 20,000 respectively. Inhibitor a acts similarly on both enzymes while inhibitor b is relatively more active on enzyme II. Storage of inhibitor b at -20 °C for several weeks resulted in a partial conversion to a lower-molecular-weight form with properties similar to those of inhibitor a. © 1985.
author	Seigelchifer, Mauricio Angel
author_facet	Seigelchifer, Mauricio Angel
author_sort	Seigelchifer, Mauricio Angel
title	The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii
title_short	The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii
title_full	The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii
title_fullStr	The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii
title_full_unstemmed	The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii
title_sort	presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, mucor rouxii
publishDate	1985
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v238_n1_p353_Seigelchifer http://hdl.handle.net/20.500.12110/paper_00039861_v238_n1_p353_Seigelchifer
work_keys_str_mv	AT seigelchifermauricioangel thepresenceoftwoheatstableinhibitorsofphosphoproteinphosphatasesinthedimorphicfungusmucorrouxii AT seigelchifermauricioangel presenceoftwoheatstableinhibitorsofphosphoproteinphosphatasesinthedimorphicfungusmucorrouxii
_version_	1768546280860024832

The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii

Ejemplares similares