Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme
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 ele...
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1981
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 06535caa a22009137a 4500 | ||
|---|---|---|---|
| 001 | PAPER-1272 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203037.0 | ||
| 008 | 190411s1981 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0019741739 | |
| 024 | 7 | |2 cas |a phosphorylase, 9035-74-9; Isoenzymes; Phosphorylases, EC 2.4.1.- | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a ABBIA | ||
| 100 | 1 | |a Sivak, M.N. | |
| 245 | 1 | 0 | |a Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme |
| 260 | |c 1981 | ||
| 270 | 1 | 0 | |m Sivak, M.N.; Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490, 1428 Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Tandecarz, Sivak, Cardini, (1978) Biochem. Biophys. Res. Commun, 82, pp. 157-164 | ||
| 504 | |a Feigin, Frederick, Wolf, (1951) Fed. Proc, 10, pp. 181-182. , 3rd ed | ||
| 504 | |a Slabnik, Frydman, (1970) Biochem. Biophys. Res. Commun, 38, pp. 709-714 | ||
| 504 | |a Frederick, De novo Synthesis of Polyglucans by a Phosphorylase Isoenzyme in Algae (1971) Physiologia Plantarum, 25, pp. 32-34 | ||
| 504 | |a Kamogawa, Fukui, Nikuni, (1968) J. Biochem, 63, pp. 361-369 | ||
| 504 | |a Burr, Nelson, (1975) Eur. J. Biochem, 56, pp. 539-546 | ||
| 504 | |a Thomas, Kaith, Schlender, Larner, (1968) Anal. Biochem, 25, pp. 486-499 | ||
| 504 | |a Tandecarz, Lavintman, Cardini, (1975) Biochim. Biophys. Acta, 399, pp. 345-355 | ||
| 504 | |a Davis, (1964) Ann. N. Y. Acad. Sci, 121, pp. 404-427 | ||
| 504 | |a Tandecarz, Lavitman, Cardini, (1→4)-α-d-glucan phosphorylase [(1→4)-α-d-glucan:orthophosphate glucosyltransferase] isoenzymes from sweet corn seed embryo (1973) Carbohydrate Research, 19, pp. 385-392 | ||
| 504 | |a Hedrick, Smith, (1968) Arch. Biochem. Biophys, 126, pp. 155-164 | ||
| 504 | |a Ziegler, Harrison, Leberman, (1974) Virology, 59, pp. 509-515 | ||
| 504 | |a Fairbanks, Steck, Wallanch, (1971) Biochemistry, 10, pp. 2606-2616 | ||
| 504 | |a Bonner, Laskey, (1974) Eur. J. Biochem, 46, pp. 83-88 | ||
| 504 | |a Laskey, Mills, (1975) Eur. J. Biochem, 56, pp. 335-341 | ||
| 504 | |a Martin, Ames, (1961) J. Biol. Chem, 236, pp. 1372-1379 | ||
| 504 | |a Lowry, Rosebrough, Farr, Randall, (1951) J. Biol. Chem, 193, pp. 265-275 | ||
| 504 | |a Hollo, Laszlo, Hoschke, Biosynthese der Stärke V.. Untersuchung der optimalen Reaktionsbedingungen der Amylose-Synthese (1965) Starch - Stärke, 17, pp. 377-381 | ||
| 504 | |a Hollo, Laszlo, Juhasz, Die Biosynthese der Stärke IX.. Die optimalen Bedingungen der Phosphorolyse (1967) Starch - Stärke, 19, pp. 246-250 | ||
| 504 | |a Hollo, Laszlo, Hoschke, Die Biosynthese der Stärke. 3. Mitteilung: Die Herstellung von Kartoffelphosphorylase großer Reinheit mittels DEAE -Cellulose- Säulenchromatographie (1964) Starch - Stärke, 16, pp. 243-246 | ||
| 504 | |a Kawaguchi, Fox, Holmes, Boyer, Preiss, (1978) Arch. Biochem. Biophys, 190, pp. 385-397 | ||
| 504 | |a Fox, Kawaguchi, Greenberg, Preiss, (1976) Biochemistry, 15, pp. 849-857 | ||
| 504 | |a Lloyd, (1976) Concanavalin A as a Tool, pp. 329-331. , H. Bittiger, H.P. Schnebli, Wiley, London | ||
| 504 | |a Lee, (1960) Biochim. Biophys. Acta, 43, pp. 18-24 | ||
| 504 | |a Iwata, Fukui, (1973) FEBS Lett, 36, pp. 222-226 | ||
| 504 | |a Illingworth, Brown, Cori, (1961) Proc. Nat. Acad. Sci. USA, 47, pp. 469-478. , 3rd ed | ||
| 504 | |a Tsai, Nelson, (1969) Plant Physiol, 44, pp. 159-167 | ||
| 504 | |a Frydman, Slabnik, (1973) Ann. N. Y. Acad. Sci, 210, pp. 153-169 | ||
| 504 | |a Fredrick, (1975) Plant Sci. Lett, 5, pp. 131-135 | ||
| 520 | 3 | |a 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. |l eng | |
| 593 | |a Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490, 1428 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ISOENZYME |
| 690 | 1 | 0 | |a PHOSPHORYLASE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a ENZYME SPECIFICITY |
| 690 | 1 | 0 | |a ENZYMOLOGY |
| 690 | 1 | 0 | |a HEAT |
| 690 | 1 | 0 | |a ISOLATION AND PURIFICATION |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a PLANT |
| 690 | 1 | 0 | |a HEAT |
| 690 | 1 | 0 | |a ISOENZYMES |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a PHOSPHORYLASES |
| 690 | 1 | 0 | |a PLANTS |
| 690 | 1 | 0 | |a SUBSTRATE SPECIFICITY |
| 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. 525-536 |k n. 2 |p Arch. Biochem. Biophys. |x 00039861 |w (AR-BaUEN)CENRE-1377 |t Archives of Biochemistry and Biophysics | |
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| 856 | 4 | 0 | |u https://doi.org/10.1016/0003-9861(81)90396-9 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_00039861_v212_n2_p525_Sivak |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v212_n2_p525_Sivak |y Registro en la Biblioteca Digital |
| 961 | |a paper_00039861_v212_n2_p525_Sivak |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 963 | |a VARI | ||
| 999 | |c 62225 | ||