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Abstract:

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.

Registro:

Documento: Artículo
Título:The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii
Autor:Seigelchifer, M.A.; Passeron, S.
Filiación:Programa de Regulación Hormonal y Metabólica, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Pabellón 2, 1428 Buenos Aires, Argentina
Palabras clave: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
Año:1984
Volumen:229
Número:1
Página de inicio:403
Página de fin:413
DOI: http://dx.doi.org/10.1016/0003-9861(84)90170-X
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:manganese, 16397-91-4, 7439-96-5; phosphoprotein phosphatase, 9025-75-6; Manganese, 7439-96-5; Phosphoprotein Phosphatase, EC 3.1.3.16
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v229_n1_p403_Seigelchifer

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Citas:

---------- APA ----------
Seigelchifer, M.A. & Passeron, S. (1984) . The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii. Archives of Biochemistry and Biophysics, 229(1), 403-413.
http://dx.doi.org/10.1016/0003-9861(84)90170-X
---------- CHICAGO ----------
Seigelchifer, M.A., Passeron, S. "The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii" . Archives of Biochemistry and Biophysics 229, no. 1 (1984) : 403-413.
http://dx.doi.org/10.1016/0003-9861(84)90170-X
---------- MLA ----------
Seigelchifer, M.A., Passeron, S. "The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii" . Archives of Biochemistry and Biophysics, vol. 229, no. 1, 1984, pp. 403-413.
http://dx.doi.org/10.1016/0003-9861(84)90170-X
---------- VANCOUVER ----------
Seigelchifer, M.A., Passeron, S. The separation and properties of two phosphoprotein phosphatases from the dimorphic fungus Mucor rouxii. Arch. Biochem. Biophys. 1984;229(1):403-413.
http://dx.doi.org/10.1016/0003-9861(84)90170-X