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Abstract:

Phosphorylase II from potato tuber has been subjected to several purification procedures in order to: (a) separate the unprimed activity from the primed one coexisting in the enzymatic preparation, and (b) eliminate endogenous glucan and/or glycoproteins. Large-scale analytical nondenaturing gel electrophoresis and affinity chromatography on concanavalin A-Sepharose 4B succeeded in removing endogenous glycoproteins without any effect on the unprimed activity. In addition, phosphorolysis or glucoamylase treatment of the enzymatic preparation did not abolish the phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. However, no separation between both activities, primed and unprimed, could be achieved either by the above-mentioned methods or by sucrose density gradient centrifugation. Based on sodium dodecyl sulfate-urea-gel electrophoresis, a molecular weight of about 96,000 was found for the phosphorylase II subunit. Molecular weight determination by nondenaturing gel electrophoresis at 5, 6, 7, and 8% acrylamide and by ultracentrifugation on sucrose density gradients suggested that the native enzyme is a dimer, as are other phosphorylases. © 1981.

Registro:

Documento: Artículo
Título:Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme
Autor:Sivak, M.N.; Tandecarz, J.S.; Cardini, C.E.
Filiación:Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:isoenzyme; phosphorylase; article; enzyme specificity; enzymology; heat; isolation and purification; kinetics; metabolism; molecular weight; plant; Heat; Isoenzymes; Kinetics; Molecular Weight; Phosphorylases; Plants; Substrate Specificity; Support, Non-U.S. Gov't
Año:1981
Volumen:212
Número:2
Página de inicio:525
Página de fin:536
DOI: http://dx.doi.org/10.1016/0003-9861(81)90396-9
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:phosphorylase, 9035-74-9; Isoenzymes; Phosphorylases, EC 2.4.1.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v212_n2_p525_Sivak

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Citas:

---------- APA ----------
Sivak, M.N., Tandecarz, J.S. & Cardini, C.E. (1981) . Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme. Archives of Biochemistry and Biophysics, 212(2), 525-536.
http://dx.doi.org/10.1016/0003-9861(81)90396-9
---------- CHICAGO ----------
Sivak, M.N., Tandecarz, J.S., Cardini, C.E. "Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme" . Archives of Biochemistry and Biophysics 212, no. 2 (1981) : 525-536.
http://dx.doi.org/10.1016/0003-9861(81)90396-9
---------- MLA ----------
Sivak, M.N., Tandecarz, J.S., Cardini, C.E. "Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme" . Archives of Biochemistry and Biophysics, vol. 212, no. 2, 1981, pp. 525-536.
http://dx.doi.org/10.1016/0003-9861(81)90396-9
---------- VANCOUVER ----------
Sivak, M.N., Tandecarz, J.S., Cardini, C.E. Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme. Arch. Biochem. Biophys. 1981;212(2):525-536.
http://dx.doi.org/10.1016/0003-9861(81)90396-9