Glycoprotein synthesis in plants. III. Interaction between UDP-N- acetylglucosamine and GDP-mannose as substrates
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- 10181
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CIAT Library Document collection CINFOS | Document Collection CINFOS | 10181 (Browse shelf(Opens below)) | c.1 | Short Loan | 100042460 |
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Este informe presenta evidencia de que las enzimas presentes en extractos crudos de los cotiledones en desarrollo de Phaseolus vulgaris pueden catalizar la transferencia de radioactividad del uridina difosfato (UDP)-N_[C(14)] acetilglucosamina a los siguientes compuestos: lipido-quitobiosil, lipido-oligosacarido y glicroproteinas. La evidencia cinetica confirma el concepto de que los lipidos que contienen N-acetilglucosamina son precursores de la glicoproteina. Tambien se presenta evidencia que demuestra una interaccion entre la GDP-manosa y la UDP-N-acetilglucosamina cuando se usan como substratos para sintesis de lipido-oligasacarido y de glicoproteina. La evidencia cinetica, asi como el aislamiento y caracterizacion de los oligasacaridos liberados del lipido por la hidrolisis acida, confirman la conclusion de que la manosa y la N- acetilglucosamina se encuentran contenidas en el mismo oligosacarido y que la N-acetilglucosamina esta presente en el extremo reductor del oligasacarido. Noventa y ocho por ciento de la radioactividad del UDP-N-[C(14)] acetilglucosamina es incorporada en el residuo insoluble, el cual es solubilizado por el tratamiento con proteasa. El glicopeptido liberado es bastante similar en tamano y composicion al glicopeptido liberado por la digestion proteolitica de la vicilina, la principal proteina de almacenamiento de P. vulgaris. (RA-CIAT) spa
Evidence is presented that enzymes present in crude extracts prepared from developing cotyledons of Phaseolus vulgaris can catalyze the transfer of radioactivity from UDP-N[(14)C] acetylglucosamine into a chitobiosyl-lipid, lipid-oligosaccharide and glycoprotein. Kinetic evidence supports the concept that the N- acetylglucosamine-containing lipids are precursors to the glycoprotein. There is also an interaction between GDP-mannose and UDP-N-acetylglucosamine when used as substrates for the synthesis of lipid-oligosaccharide and glycoprotein. Kinetic evidence, as well as isolation and characterization of the oligosaccharides released from lipid by mild acid hydrolyses, supports the conclusion that mannose and N-acetylglucosamine are contained in the same oligosaccharide and that N-acetylglucosamine is present at the reducing end of the oligosaccharide. Of the radioactivity incorporated from UDP-N[(14)C] acetylglucosamine into the insoluble residue, 98 percent is solubilized by protease treatment. The glycopeptide released is quite similar in size and composition to the glycopeptide released by proteolytic digestion of vicilin, the major storage protein of P. vulgaris. (AS) eng