Adenosine diphosphate glucose and starch synthesis

originalFil: Recondo, Eduardo F.. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Leloir, Luis Federico. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaBlanco y negro2 páginas en pdfLFL-PI-O-ART. Artículos científicosUnidad documental simpleAR-HYL-201

Isolation of adenosine diphosphate D-glucose from corn grains

originalFil: Recondo, Eduardo F.. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Dankert, Marcelo. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Leloir, Luis Federico. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaBlanco y negro2 páginas en pdfLFL-PI-O-ART. Artículos científicosUnidad documental simpleAR-HYL-201

21 de setiembre: día de la ciencia y la técnica

Con motivo del 3O aniversario de la instauración del 21 de setiembre como día de la Ciencia y la Técnica en la Provincia de Buenos Aires, la CIC le ha solicitado a un grupo selecto de científicos, su opinión sobre aspectos esenciales del quehacer científico y tecnológico. El presente texto contiene los siguientes trabajos: - Consideraciones acerca de la investigacion técnico-científica sobre materiales, por Eduardo R. Abril. - Ciencia y tecnología de alimentos, por Pedro Cattáneo - Ciencia y tecnología en química orgánica por Venancio Deulofeu. - Ciencia y tecnología - recursos humanos por Ernesto E. Galloni. - Discurso de apertura de la reunion sobre ciencia y tecnologia realizada en Mar del Plata del 6 al 8 de julio de 1978 por Luis F. Leloir. - Incidencia de la investigación en el desarrollo de la metalurgia por Roberto F. Recoder. - Importancia de la investigación matemática en la sociedad contemporánea por Luis A. Santaló. - La investigación en fisicoquímica y su proyección en el desarrollo científico y tecnológico por Hans J. Schumacher

Action of glycosidases on the saccharide moiety of the glucose—containing dolichyl diphosphate oligosaccharide

originalFil: Ugalde, Rodolfo Augusto. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Staneloni, Roberto Julio. Instituto de Investigaciones Bioquímicas Fundación Campomar; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Leloir, Luis Federico. Instituto de Investigaciones Bioquímicas Fundación Campomar; Argentinablanco y negro1 ejemplarLFL-PI-O-ART. Artículos científicosUnidad documental simpleAR-HYL-201

Subcellular distribution of dolichol phosphate

originalFil: Dallner, Gustav. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Behrens, Nicolás H.. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Parodi, Armando José A.. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Leloir, Luis Federico. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaBlanco y negro3 páginas en pdfLFL-PI-O-ART. Artículos científicosUnidad documental simpleAR-HYL-201

Dolichyl monophosphate and its sugar derivatives in plants.

A glucose acceptor was isolated from soya beans by extraction with chloroform/methanol (2:1, v/v), followed by DEAE-cellulose column chromatography of the extract. This acceptor could not be distinguished from liver dolichyl monophosphate by t.l.c. It could replace dolichyl monophosphate as a mannose acceptor with a liver enzyme and its glucosylated derivative could replace dolichyl monophosphate glucose as a glucose donor in the same system. These results, together with those already reported [Pont Lezica, Brett, Romero Martinez & Dankert (1975) Biochem, Biophys. Res. Commun. 66, 980-987], indicate that the acceptor from soya bean is a dolichyl monophosphate. Gel filtration of its glucosylated derivative on Sephadex G-75 in the presence of sodium deoxycholate indicated that the acceptor contained 17 or 18 isoprene units. An enzyme preparation from pea seedlings was shown to use endogenous acceptors to form lipid phosphate sugars containing mannose and N-acetylglucosamine from GDP-mannose and UDP-N-acetylglucosamine. Chromatographic and degradative techniques indicated that the compounds formed were lipid monophosphate mannose, lipid pyrophosphate N-acetylglucosamine, lipid pyrophosphate chitobiose and a series of lipid pyrophosphate oligosaccharides containing both mannose and N-acetylglucosamine. None of these compounds was degraded by catalytic hydrogenation, and so the lipid moiety in each case was probably an alpha-saturated polyprenol. The endogenous acceptors for mannose and N-acetylglucosamine in peas may therefore be dolichyl monophosphate, as has been found in mammalian systems

Oligosaccharides containing glucose and mannose in glycoproteins of the thyroid gland.

The glucose-containing oligosaccharides formed by calf thyroid slices incubated with radioactive glucose were studied. A compound soluble in chloroform/methanol/water, 1:1:0.3 (vol/vol), was found that was indistinguishable from the previously described glucose-containing dolichyl diphosphate oligosaccharide formed by liver microsomes. Glycopeptides were prepared by treating the glycoproteins with pronase, the amino acids were removed with alkaline borohydride, and the products were examined by paper electrophoresis and chromatography. A saccharide equal to that which occurs in the glucose-containing dolichyl diphosphate oligosaccharide could not be detected but glucose was found in oligosaccharides that seemed to be smaller by about three to five monosaccharide residues. The same results were obtained by direct treatment of the glycoproteins with alkaline borohydride