Biosynthesis of paramylon in Euglena gracilis

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Detalles Bibliográficos
Autor principal: Goldemberg, S.H
Otros Autores: Marechal, L.R
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1963
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-s2.0-4243783100 
024 7 |2 cas  |a Polysaccharides 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
100 1 |a Goldemberg, S.H. 
245 1 0 |a Biosynthesis of paramylon in Euglena gracilis 
260 |c 1963 
270 1 0 |m Goldemberg, S.H.; Instituto de Investigaciones Bioquímicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
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: In order to identify the reaction product, the radioactive material was hydrolyzed with HC1 as indicated in Fig. I. It can be seen that the location of the radioactive spots corresponds with that of the oligosaccharides formed from similarly hydrolyzed laminarin, another/3-1,3-glucan, and also with that of authentic glucose, laminaribiose and laminaritriose. The radioactive product was also degraded enzymically using laminarase, a fl-I,3-glucan hydrolase obtained from E. gracilis 5. Radioactivity determinations showed that 519o of tile original counts were recovered in the supernatant after laminarase action. When chromatographed, these counts were located in the zone corresponding to glucose. Under the conditions of the experiment, laminarase hydrolyzed 4 ° % of the original paramylon* and only 2 % of starch, 1% of glycogen and 1% of soluble cellodextrin. The enzyme seems to quite specific for UDP-~-glucose. Thus adenosine diphosphate glucose was 25 % and deoxyadenosine diphosphate glucose 15 °o as effective as UDP-a-glucose, while with UDP-fl-glucose no activity could be detected. Further studies on the enzyme are being carried out. This investigation was supported in part by a research grant (No. G-3442) from tile National Institutes of Health, U.S. Public Health Service, by the Rockefeller Foundation and by the Consejo Nacional de Investigaciones Cientfficas y T6cnicas. Thanks are due to Dr. L. F. LELOIR for his continued interest and support and to all the members of the Instituto de Investigaciones Bioquimicas for their collaboration. 
593 |a Instituto de Investigaciones Bioquímicas Fundacion Campomar, Facultad de Ciencias Exactas y Naturales, Buenos Aires, Argentina 
690 1 0 |a POLYSACCHARIDE 
690 1 0 |a ARTICLE 
690 1 0 |a EUGLENA 
690 1 0 |a EUGLENA 
690 1 0 |a POLYSACCHARIDES 
690 1 0 |a EUGLENA 
690 1 0 |a POLYSACCHARIDES 
700 1 |a Marechal, L.R. 
773 0 |d 1963  |g v. 71  |h pp. 743-744  |k n. C  |x 00063002  |w (AR-BaUEN)CENRE-164  |t BBA - Biochimica et Biophysica Acta 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00063002_v71_nC_p743_Goldemberg  |y Handle 
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