a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver

a-1,4-glucan:a-1,4-glucan 6-glycosyltransferase was purified about 35-fold from rat-liver extracts. Removal of α-amylase could be accomplished by high-speed centrifugation of extracts from livers with high glycogen content. Enzyme action on amylopectin is optimum at pH 6.4 in 0.3 M citrate buffer. I...

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Detalles Bibliográficos
Autor principal: Krisman, C.R
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1962
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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024 7 |2 scopus  |a 2-s2.0-9844232718 
024 7 |2 cas  |a glucosyltransferase, 9031-48-5; Glucosyltransferases, 2.4.1.- 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
100 1 |a Krisman, C.R. 
245 1 0 |a a-1,4-glucan: a-1,4-glucan 6-glycosyltransferase from liver 
260 |c 1962 
270 1 0 |m Krisman, C.R.; Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
520 3 |a a-1,4-glucan:a-1,4-glucan 6-glycosyltransferase was purified about 35-fold from rat-liver extracts. Removal of α-amylase could be accomplished by high-speed centrifugation of extracts from livers with high glycogen content. Enzyme action on amylopectin is optimum at pH 6.4 in 0.3 M citrate buffer. It requires salts for maximal activity, and is inhibited by molybdate, Mn2+, Mg2+ and sodium p-chloromercuribenzoate. Amylose and amylopectin ß-limit dextrin were also substrates for the liver branching enzyme. A method is described for the assay of the enzyme in the presence of α-amylase. © 1962.  |l eng 
536 |a Detalles de la financiación: U.S. Public Health Service 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, T6cnicas 
536 |a Detalles de la financiación: National Institutes of Health 
536 |a Detalles de la financiación: Rockefeller Foundation 
536 |a Detalles de la financiación: I wish to express my gratitude to Dr. L. F. LELOIR for his inspiring guidance and support, and to the other members of the Instituto de Investigaciones Bioquimicas "Fundaci6n Campomar" for many helpful discussions and criticisms, This investigation was supported in part by a research grant (No G-3442) from the National Institutes of Health, U.S. Public Health Service, by the Rockefeller Foundation and by the Consejo Nacional de Investigaciones Cientificas y T6cnicas. The author is an investigator of the Instituto Nacional de Microbiologla. 
593 |a Instituto de Investigaciones Bioquimicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina 
690 1 0 |a GLUCOSYLTRANSFERASE 
690 1 0 |a ARTICLE 
690 1 0 |a LIVER 
690 1 0 |a GLUCOSYLTRANSFERASES 
690 1 0 |a LIVER 
690 1 0 |a GLUCOSYLTRANSFERASES 
690 1 0 |a LIVER 
773 0 |d 1962  |g v. 65  |h pp. 307-315  |k n. 2  |x 00063002  |w (AR-BaUEN)CENRE-164  |t BBA - Biochimica et Biophysica Acta 
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856 4 0 |u https://doi.org/10.1016/0006-3002(62)91049-1  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00063002_v65_n2_p307_Krisman  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00063002_v65_n2_p307_Krisman  |y Registro en la Biblioteca Digital 
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999 |c 62724