Studies on potato tuber phosphorylase catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product

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 enz...

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Autor principal: Sivak, M.N
Otros Autores: Tandecarz, J.S, Cardini, C.E
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1981
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Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0019760924 
024 7 |2 cas  |a 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.- 
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100 1 |a Sivak, M.N. 
245 1 0 |a Studies on potato tuber phosphorylase catalyzed reaction in the absence of an exogenous acceptor. II. Characterization of the reaction product 
260 |c 1981 
270 1 0 |m Sivak, M.N.; Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490, 1428 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Lavintman, Cardini, (1972) Biochemistry of the Glycosidic Linkage, pp. 503-507. , R. Piras, H.G. Pontis, Academic Press, New York 
504 |a Lavintman, Cardini, (1973) FEBS Lett, 29, pp. 43-46 
504 |a Lavintman, Tandecarz, Carceller, Mendiara, Cardini, (1974) Eur. J. Biochem, 50, pp. 145-155 
504 |a Tandecarz, Cardini, (1978) Biochim. Biophys. Acta, 543, pp. 423-429 
504 |a Tandecarz, Cardini, (1979) Plant Sci. Lett, 15, pp. 151-158 
504 |a Krisman, (1972) Biochem. Biophys. Res. Commun, 46, pp. 1206-1212 
504 |a Krisman, Barengo, (1975) Eur. J. Biochem, 52, pp. 117-123 
504 |a Barengo, Flawia, Krisman, (1975) FEBS Lett, 53, pp. 274-278 
504 |a Tomos, Northcote, (1978) Biochem. J, 174, pp. 283-290 
504 |a Tandecarz, J. S., Lavintman, N., Cardini, C. E. (175) Biochim. Biophys. Acta399, 345-355; Tandecarz, Sivak, Cardini, (1978) Biochim. Biophys. Res. Commun, 82, pp. 157-164 
504 |a Sivak, Tandecarz, Cardini, (1981) Arch. Biochem. Biophys, 212, pp. 525-536 
504 |a Panayotatos, Villemez, (1973) Biochem. J, 133, pp. 263-271 
504 |a Trevelyan, Procter, Harrison, (1950) Nature (London), 166, pp. 444-445 
504 |a Hedrick, Smith, (1968) Arch. Biochem. Biophys, 126, pp. 155-164 
504 |a Holmes, Preiss, (1979) Arch. Biochem. Biophys, 196, pp. 436-448 
504 |a Bailey, Whelan, (1961) J. Biol. Chem, 236, pp. 969-973 
504 |a Segrest, Jackson, (1972) Methods in Enzymology, 28, pp. 54-63. , 3rd ed., V. Ginsburg, Academic Press, New York 
504 |a Goldstein, Hollerman, Merrick, (1965) Biochim. Biophys. Acta, 97, pp. 68-76 
504 |a Lloyd, (1976) Concanavalin A as a Tool, pp. 323-331. , H. Bittiger, H.P. Schnebli, Wiley, London 
504 |a Geisow, (1979) Nature (London), 281, pp. 15-16 
520 3 |a 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.  |l eng 
593 |a Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490, 1428 Buenos Aires, Argentina 
650 1 7 |2 spines  |a CARBON 
690 1 0 |a GLUCAN 
690 1 0 |a GLUCOSE 1 PHOSPHATE 
690 1 0 |a GLUCOSE PHOSPHATE 
690 1 0 |a GLYCOPROTEIN 
690 1 0 |a ISOENZYME 
690 1 0 |a PHOSPHORYLASE 
690 1 0 |a AFFINITY CHROMATOGRAPHY 
690 1 0 |a ARTICLE 
690 1 0 |a DENSITY GRADIENT CENTRIFUGATION 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a ISOLATION AND PURIFICATION 
690 1 0 |a METABOLISM 
690 1 0 |a MOLECULAR WEIGHT 
690 1 0 |a PLANT 
690 1 0 |a POLYACRYLAMIDE GEL ELECTROPHORESIS 
690 1 0 |a CARBON RADIOISOTOPES 
690 1 0 |a CENTRIFUGATION, DENSITY GRADIENT 
690 1 0 |a CHROMATOGRAPHY, AFFINITY 
690 1 0 |a ELECTROPHORESIS, POLYACRYLAMIDE GEL 
690 1 0 |a GLUCANS 
690 1 0 |a GLUCOSEPHOSPHATES 
690 1 0 |a GLYCOPROTEINS 
690 1 0 |a ISOENZYMES 
690 1 0 |a MOLECULAR WEIGHT 
690 1 0 |a PHOSPHORYLASES 
690 1 0 |a PLANTS 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
700 1 |a Tandecarz, J.S. 
700 1 |a Cardini, C.E. 
773 0 |d 1981  |g v. 212  |h pp. 537-545  |k n. 2  |p Arch. Biochem. Biophys.  |x 00039861  |w (AR-BaUEN)CENRE-1377  |t Archives of Biochemistry and Biophysics 
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