Adenosine diphosphate glucose: Orthophosphate adenylyltransferase in wheat germ

An enzyme has been isolated from wheat germ which catalyzes the reaction: ADP-sugar + inorganic phosphate → ADP + sugar phosphate. Maximal activity was found at pH 8-9. The equilibrium of the reaction seems to be completely displaced towards ADP formation. The enzyme acts on ADP-glucose and deADP-gl...

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Detalles Bibliográficos
Autor principal: Dankert, M.
Otros Autores: Ruth, I., Gonçalves, J., Recondo, E.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1964
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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100 1 |a Dankert, M. 
245 1 0 |a Adenosine diphosphate glucose: Orthophosphate adenylyltransferase in wheat germ 
260 |c 1964 
270 1 0 |m Dankert, M.; Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
520 3 |a An enzyme has been isolated from wheat germ which catalyzes the reaction: ADP-sugar + inorganic phosphate → ADP + sugar phosphate. Maximal activity was found at pH 8-9. The equilibrium of the reaction seems to be completely displaced towards ADP formation. The enzyme acts on ADP-glucose and deADP-glucose and more slowly, on ADP-xylose and ADP-β-glucose. Evidence is presented indicating that inorganic phosphate is incorporated in the terminal position of the nucleotide. Arsenate can be substituted for inorganic phosphate, AMP being the final product. © 1964.  |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 
536 |a Detalles de la financiación: National Institutes of Health 
536 |a Detalles de la financiación: Rockefeller Foundation 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: The authors are deeply indebted to Drs. H. CARMINATTI, H. N. TORRES and C. E. CARDINI for advice and helpful criticism; to Dr. L. F. LELOIR for his help in the English version and continued support and to the other members of the Instituto de Investigaciones Bioquimicas for valuable criticism. 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 (Argentina). 
536 |a Detalles de la financiación: M.D. is a Fellow of the Consejo Nacional de Investigaciones Cientificas y T6cnicas (Argey!tina). I. R. J. G. is a Post-graduate Fellow of the Gov~rno do Estado de Rio Grande do Sul (Brasil). E. R. is a Career Fellow of the Consejo Nacional de Investigaciones Cientificas y T~cnicas. 
593 |a Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires, Argentina 
700 1 |a Ruth, I. 
700 1 |a Gonçalves, J. 
700 1 |a Recondo, E. 
773 0 |d 1964  |g v. 81  |h pp. 78-85  |k n. 1  |x 09266569  |w (AR-BaUEN)CENRE-970  |t BBA - Enzymological Subjects 
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