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Abstract:

Branching enzymes from rat and rabbit liver, as well as from potato and maize were prepared. They were almost free from contaminating glucan‐degrading enzymes. In ‘sweet corn’ maize, two separate fractions with (α1,4)glucan: (α1,4)glucan α6‐glycosyltransferase activities were obtained. One of them synthesized amylopectin, the branched component of starch, in the presence of phosphorylase and Glc1P, while the other fraction synthesized phytoglycogen. Furthermore, in a maize variety which does not accumulate phytoglycogen, only one fraction of branching activity was found, that formed amylopectin under the above‐mentioned conditions. Comparative analyses performed with native (α1,4)‐(α1,6)glucopolysaccharides, and those synthesized in vitro with the branching enzyme from the same tissue, demonstrated a close similarity between both glucans. It may be concluded that the branching enzyme is responsible for the specific degree of (α1,6) branch linkages found in the native polysaccharide. Copyright © 1987, Wiley Blackwell. All rights reserved

Registro:

Documento: Artículo
Título:The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes
Autor:Tolmasky, D.S.; Krisman, C.R.
Filiación:Instituto de Investigaciones Bioquimicas 'Fundacion Campomar', Facultad de Ciencias Exactas y Naturales and CONICET Buenos Aires, Argentina
Palabras clave:1,4 alpha glucan branching enzyme; amylopectin; elongation factor; glucosyltransferase; glycogen synthase; phosphorylase; polysaccharide; animal; article; atomic absorption spectrometry; biosynthesis; enzymology; glycogen liver level; in vitro study; liver; maize; metabolism; potato; rabbit; rat; structure activity relation; 1,4-alpha-Glucan Branching Enzyme; Amylopectin; Animal; Glucosyltransferases; Glycogen Synthase; In Vitro; Liver; Liver Glycogen; Peptide Elongation Factors; Phosphorylases; Polysaccharides; Potatoes; Rabbits; Rats; Spectrophotometry, Atomic Absorption; Structure-Activity Relationship; Support, Non-U.S. Gov't; Zea mays
Año:1987
Volumen:168
Número:2
Página de inicio:393
Página de fin:397
DOI: http://dx.doi.org/10.1111/j.1432-1033.1987.tb13432.x
Título revista:European Journal of Biochemistry
Título revista abreviado:Eur. J. Biochem.
ISSN:00142956
CAS:1,4 alpha glucan branching enzyme, 9001-97-2; amylopectin, 9037-22-3; glucosyltransferase, 9031-48-5; glycogen synthase, 9033-05-0; phosphorylase, 9035-74-9; 1,4-alpha-Glucan Branching Enzyme, EC 2.4.1.18; Amylopectin, 9037-22-3; Glucosyltransferases, EC 2.4.1.-; Glycogen Synthase, EC 2.4.1.11; Liver Glycogen; Peptide Elongation Factors; Phosphorylases, EC 2.4.1.-; Polysaccharides
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v168_n2_p393_Tolmasky

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Citas:

---------- APA ----------
Tolmasky, D.S. & Krisman, C.R. (1987) . The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes. European Journal of Biochemistry, 168(2), 393-397.
http://dx.doi.org/10.1111/j.1432-1033.1987.tb13432.x
---------- CHICAGO ----------
Tolmasky, D.S., Krisman, C.R. "The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes" . European Journal of Biochemistry 168, no. 2 (1987) : 393-397.
http://dx.doi.org/10.1111/j.1432-1033.1987.tb13432.x
---------- MLA ----------
Tolmasky, D.S., Krisman, C.R. "The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes" . European Journal of Biochemistry, vol. 168, no. 2, 1987, pp. 393-397.
http://dx.doi.org/10.1111/j.1432-1033.1987.tb13432.x
---------- VANCOUVER ----------
Tolmasky, D.S., Krisman, C.R. The degree of branching in (α1,4)‐(α1,6)‐linked glucopolysaccharides is dependent on intrinsic properties of the branching enzymes. Eur. J. Biochem. 1987;168(2):393-397.
http://dx.doi.org/10.1111/j.1432-1033.1987.tb13432.x