Studies on the biosynthesis of starch. I. Isolation and properties of the soluble adenosine diphosphate glucose: Starch glucosyltransferase of Solanum tuberosum

A soluble glucan synthetase (starch synthetase) has been isolated from potato tubers. This enzyme catalyzes the transfer of glucose from adenosine diphosphate glucose, deoxyadenosine diphosphate glucose, and to a lesser extent, from β-adenosine diphosphate glucose to phytoglycogen, amylopectin, and...

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Detalles Bibliográficos
Autor principal: Frydman, R.B
Otros Autores: Cardini, C.E
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1966
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0014028939 
024 7 |2 cas  |a glucose, 50-99-7, 84778-64-3; glucosyltransferase, 9031-48-5; glycogen, 9005-79-2; pectin, 9000-69-5; starch, 9005-25-8, 9005-84-9; Adenine Nucleotides; Glucose, 50-99-7; Glucosyltransferases, EC 2.4.1.-; Glycogen, 9005-79-2; Oligosaccharides; Pectins; Starch, 9005-25-8 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a ABBIA 
100 1 |a Frydman, R.B. 
245 1 0 |a Studies on the biosynthesis of starch. I. Isolation and properties of the soluble adenosine diphosphate glucose: Starch glucosyltransferase of Solanum tuberosum 
260 |c 1966 
270 1 0 |m Frydman, R.B.; Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina 
506 |2 openaire  |e Política editorial 
520 3 |a A soluble glucan synthetase (starch synthetase) has been isolated from potato tubers. This enzyme catalyzes the transfer of glucose from adenosine diphosphate glucose, deoxyadenosine diphosphate glucose, and to a lesser extent, from β-adenosine diphosphate glucose to phytoglycogen, amylopectin, and malto-oligosaccharides. β-Limit dextrins, dextran, and isomalto-oligosaccharides were inactive as primers. The freshly prepared enzyme also catalyzes the transfer of glucose from the sugar nucleotide to the intact starch granules, but this activity disappears with storage. The properties of the enzyme which acts on the soluble primers were studied. © 1966.  |l eng 
536 |a Detalles de la financiación: National Institutes of Health 
536 |a Detalles de la financiación: Rockefeller Foundation 
536 |a Detalles de la financiación: U.S. Public Health Service 
536 |a Detalles de la financiación: 1 This investigation was supported in part by a research grant (GM 03442) from t,he National Institutes of Health, United States Public Health Service; by the Rockefeller Foundation; and by the Consejo National de Investigaciones Cientifi-cas y T&micas (Repdblica Argent’ina). 2 Career investigator of the Consejo de Investignciones Cientificas y Titcnicas. 
593 |a Instituto de Investigaciones Bioquímicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina 
690 1 0 |a ADENINE NUCLEOTIDE 
690 1 0 |a GLUCOSE 
690 1 0 |a GLUCOSYLTRANSFERASE 
690 1 0 |a GLYCOGEN 
690 1 0 |a OLIGOSACCHARIDE 
690 1 0 |a PECTIN 
690 1 0 |a STARCH 
690 1 0 |a ARTICLE 
690 1 0 |a BIOSYNTHESIS 
690 1 0 |a CHEMISTRY 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a IN VITRO STUDY 
690 1 0 |a KINETICS 
690 1 0 |a METABOLISM 
690 1 0 |a PLANT 
690 1 0 |a ADENINE NUCLEOTIDES 
690 1 0 |a CHEMISTRY 
690 1 0 |a GLUCOSE 
690 1 0 |a GLUCOSYLTRANSFERASES 
690 1 0 |a GLYCOGEN 
690 1 0 |a IN VITRO 
690 1 0 |a KINETICS 
690 1 0 |a OLIGOSACCHARIDES 
690 1 0 |a PECTINS 
690 1 0 |a PLANTS, EDIBLE 
690 1 0 |a STARCH 
700 1 |a Cardini, C.E. 
773 0 |d 1966  |g v. 116  |h pp. 9-18  |k n. C  |p Arch. Biochem. Biophys.  |x 00039861  |w (AR-BaUEN)CENRE-1377  |t Archives of Biochemistry and Biophysics 
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