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Abstract:

Incubation of potato tuber phophorylase II with [14C]glucose 1-phosphate in the absence of an exogenous acceptor results in the synthesis of a radioactive product, presumably a protein-bound glucan. The carbohydrate moiety of this product was shown to consist of long α-1,4-glucosidic chains. The enzyme itself was originally assumed to be the first glucosyl acceptor in the unprimed reaction. However, as judged by urea-sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the radioactive product is rather resistant to proteolysis and is smaller in size than phosphorylase II. These data are in agreement with those obtained by sucrose density gradient centrifugation and molecular-weight estimation of native products. Thus, some kind of processing postglucosylation has to be proposed to account for the observed decrease in molecular weight. One cannot overlook the probable presence of a low-molecular-weight protein acceptor which copurifies along with phosphorylase II and whose separation from the enzyme can only be achieved upon glucosylation. On the other hand, protein was also found to be present in amylose from potato starch grains. It is therefore suggested that this finding might become an additional evidence of a common biosynthetic pathway for α-1,4-glucans from a precursor protein. © 1981.

Registro:

Documento: Artículo
Título:Studies on potato tuber phosphorylase catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product
Autor:Sivak, M.N.; Tandecarz, J.S.; Cardini, C.E.
Filiación:Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:carbon; glucan; glucose 1 phosphate; glucose phosphate; glycoprotein; isoenzyme; phosphorylase; affinity chromatography; article; density gradient centrifugation; enzymology; isolation and purification; metabolism; molecular weight; plant; polyacrylamide gel electrophoresis; Carbon Radioisotopes; Centrifugation, Density Gradient; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Glucans; Glucosephosphates; Glycoproteins; Isoenzymes; Molecular Weight; Phosphorylases; Plants; Support, Non-U.S. Gov't
Año:1981
Volumen:212
Número:2
Página de inicio:537
Página de fin:545
DOI: http://dx.doi.org/10.1016/0003-9861(81)90397-0
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:carbon, 7440-44-0; glucan, 9012-72-0, 9037-91-6; glucose 1 phosphate, 59-56-3; phosphorylase, 9035-74-9; Carbon Radioisotopes; Glucans; glucose-1-phosphate, 59-56-3; Glucosephosphates; Glycoproteins; Isoenzymes; Phosphorylases, EC 2.4.1.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v212_n2_p537_Sivak

Referencias:

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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. II. Characterization of the reaction product. Archives of Biochemistry and Biophysics, 212(2), 537-545.
http://dx.doi.org/10.1016/0003-9861(81)90397-0
---------- CHICAGO ----------
Sivak, M.N., Tandecarz, J.S., Cardini, C.E. "Studies on potato tuber phosphorylase catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product" . Archives of Biochemistry and Biophysics 212, no. 2 (1981) : 537-545.
http://dx.doi.org/10.1016/0003-9861(81)90397-0
---------- MLA ----------
Sivak, M.N., Tandecarz, J.S., Cardini, C.E. "Studies on potato tuber phosphorylase catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product" . Archives of Biochemistry and Biophysics, vol. 212, no. 2, 1981, pp. 537-545.
http://dx.doi.org/10.1016/0003-9861(81)90397-0
---------- VANCOUVER ----------
Sivak, M.N., Tandecarz, J.S., Cardini, C.E. Studies on potato tuber phosphorylase catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product. Arch. Biochem. Biophys. 1981;212(2):537-545.
http://dx.doi.org/10.1016/0003-9861(81)90397-0