Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points

Methods previously described for glycogen or amylopectin branching enzymatic activity are insufficiently sensitive and not quantitative. A new, more sensitive, specific, and quantitative one was developed. It is based upon the quantitation of the glucose residues joined by α1,6 bonds introduced by v...

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Autor principal: Krisman, C.R
Otros Autores: Tolmasky, D.S, Raffo, S.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1985
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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024 7 |2 scopus  |a 2-s2.0-0022253656 
024 7 |2 cas  |a 1,4 alpha glucan branching enzyme, 9001-97-2; 1,4-alpha-Glucan Branching Enzyme, EC 2.4.1.18; Glucans; Glucosyltransferases, EC 2.4.1.-; Polysaccharides 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a ANBCA 
100 1 |a Krisman, C.R. 
245 1 0 |a Branching enzyme assay: Selective quantitation of the α1,6-linked glucosyl residues involved in the branching points 
260 |c 1985 
270 1 0 |m Krisman, C.R.; Instituto de Investigaciones Bioquimicas Fundacion Campomar Antonio Machado 151, 1405 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Boyer, Preiss, Multiple forms of (1 → 4)-α-d-glucan, (1 → 4)-α-d-glucan-6- glycosyl transferase from developing zea mays L. Kernels (1978) Carbohydrate Research, 61, p. 321 
504 |a Brown, Brown, (1966) Methods in Enzymology, 8, p. 395. , E.F. Neufeld, V. Ginsburg, Academic Press, New York 
504 |a Krisman, (1962) Biochem. Biophys. Acta, 65, p. 301 
504 |a Krisman, Kopun, (1982) Eur. J. Cell Biol, 27, p. 18 
504 |a Krisman, (1962) Anal. Biochem, 4, p. 17 
504 |a White, Nelson, Gillard, Zingaro, (1981) Mechanisms of Saccharide Polymerization and Depolymerization, p. 265. , J.J. Marshall, Academic Press, New York 
504 |a Cowie, Greenwood, 559. Physicochemical studies on starches. Part VI. Aqueous leaching and the fractionation of potato starch (1957) Journal of the Chemical Society (Resumed), p. 2862 
504 |a Mordoh, Krisman, Leloir, (1966) Arch. Biochem. Biophys, 113, pp. 265-272 
504 |a Montgomery, (1957) Arch. Biochem. Biophys, 67, p. 378 
504 |a Ashwell, (1957) Methods in Enzymology, 3, p. 85. , S.P. Colowick, N.O. Kaplan, Academic Press, New York 
504 |a Lowry, Rosebrough, Farr, Randall, (1951) J. Biochem. Chem, 193, p. 265 
504 |a Fales, (1959) Anal. Chem, 31, p. 1898 
504 |a Fisher, Krebs, (1962) Methods in Enzymology, 5, p. 369. , S.P. Colowick, N.O. Kaplan, Academic Press, New York 
504 |a Brown, Brown, (1966) Methods in Enzymology, 7, p. 515. , S.P. Colowick, N.O. Kaplan, Academic Press, New York 
504 |a Borovsky, Smith, Whelan, (1975) Eur. J. Biochem, 59, p. 615 
504 |a Leloir, National Cancer Institute Monograph No. 27 (1966) International Symposium on Enzymatic Aspects of Metabolic Regulation, pp. 3-18. , Mexico 
520 3 |a Methods previously described for glycogen or amylopectin branching enzymatic activity are insufficiently sensitive and not quantitative. A new, more sensitive, specific, and quantitative one was developed. It is based upon the quantitation of the glucose residues joined by α1,6 bonds introduced by varying amounts of branching enzyme. The procedure involved the synthesis of a polysaccharide from Glc-1-P and phosphorylase in the presence of the sample to be tested. The branched polysaccharide was then purified and the glucoses involved in the branching points were quantitated after degradation with phosphorylase and debranching enzymes. This method appeared to be useful, not only in enzymatic activity determinations but also in the study of the structure of α-d-glucans when combined with those of total polysaccharide quantitation, such as iodine and phenol-sulfuric acid. © 1985.  |l eng 
536 |a Detalles de la financiación: National Research Council 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: ’ Member of the Research Career of the National Research Council (CONICET), Argentina. ’ Recipient of the Fellowship “Maria Scasso de Cam-pomar.” 3 Member of the Technical Career of the National Research Council (CONICET), Argentina. 
593 |a Instituto de Investigaciones Bioquimicas Fundacion Campomar Antonio Machado 151, 1405 Buenos Aires, Argentina 
593 |a Facultad de Ciencias Exactas y Naturales, Antonio Machado 151, 1405 Buenos Aires, Argentina 
690 1 0 |a AMYLO-Α1,4-Α1,6-TRANSGLUCOSYLASE 
690 1 0 |a AMYLOPECTIN 
690 1 0 |a BRANCHING ENZYME ASSAY 
690 1 0 |a GLYCOGEN 
690 1 0 |a QUANTITATION OF BRANCHING POINTS 
690 1 0 |a Α1,6-GLUCOSYDIC LINKAGE 
690 1 0 |a 1,4 ALPHA GLUCAN BRANCHING ENZYME 
690 1 0 |a ENZYME ASSAY 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a 1,4-ALPHA-GLUCAN BRANCHING ENZYME 
690 1 0 |a ANIMAL 
690 1 0 |a GLUCANS 
690 1 0 |a GLUCOSYLTRANSFERASES 
690 1 0 |a POLYSACCHARIDES 
690 1 0 |a RABBITS 
700 1 |a Tolmasky, D.S. 
700 1 |a Raffo, S. 
773 0 |d 1985  |g v. 147  |h pp. 491-496  |k n. 2  |p Anal. Biochem.  |x 00032697  |w (AR-BaUEN)CENRE-163  |t Analytical Biochemistry 
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856 4 0 |u https://doi.org/10.1016/0003-2697(85)90303-3  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00032697_v147_n2_p491_Krisman  |y Handle 
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