A novel galacturonide from Xanthomonas campestris

Enzyme preparations from Xanthomonas campestris incubated in the presence of UDP-[14C]GlcA and Mg2+ produced a lipophilic galacturonide with unusual properties. It was easily degraded by both mild acid treatment (0.01 M-HCl, 100°C, 10 min) and mild alkali treatment (0.06 M-NaOH, room temperature, 5...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Baldessari, Alicia, Ielpi, Luis, Dankert, Marcelo Alberto
Publicado:	1990
Materias:	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas campestris
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221287_v136_n8_p1501_Baldessari http://hdl.handle.net/20.500.12110/paper_00221287_v136_n8_p1501_Baldessari
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00221287_v136_n8_p1501_Baldessari
record_format	dspace
spelling	paper:paper_00221287_v136_n8_p1501_Baldessari2025-07-30T17:28:40Z A novel galacturonide from Xanthomonas campestris Baldessari, Alicia Ielpi, Luis Dankert, Marcelo Alberto polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris Enzyme preparations from Xanthomonas campestris incubated in the presence of UDP-[14C]GlcA and Mg2+ produced a lipophilic galacturonide with unusual properties. It was easily degraded by both mild acid treatment (0.01 M-HCl, 100°C, 10 min) and mild alkali treatment (0.06 M-NaOH, room temperature, 5 min) releasing free [14C]galacturonic acid. The galacturonide appeared to be a single compound with one negative charge, as judged by TLC, paper electrophoresis and chromotography, LH-20 gel filtration and DEAE-cellulose column chromatography. Competition experiments indicated that the true glycosyl donor was UDP-GalA, in agreement with the detection of UDP-GlcA-4-epimerase activity in the crude enzyme preparation. The transglycosidase activity was located mainly in the membrane fraction. UDP inhibited the reaction and even produced some loss of label, suggesting an easily reversible reaction. UMP had almost no effect. Fil:Baldessari, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ielpi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Dankert, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1990 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221287_v136_n8_p1501_Baldessari http://hdl.handle.net/20.500.12110/paper_00221287_v136_n8_p1501_Baldessari
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris
spellingShingle	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris Baldessari, Alicia Ielpi, Luis Dankert, Marcelo Alberto A novel galacturonide from Xanthomonas campestris
topic_facet	polysaccharide radioisotope article nonhuman priority journal Xanthomonas Xanthomonas Xanthomonas campestris
description	Enzyme preparations from Xanthomonas campestris incubated in the presence of UDP-[14C]GlcA and Mg2+ produced a lipophilic galacturonide with unusual properties. It was easily degraded by both mild acid treatment (0.01 M-HCl, 100°C, 10 min) and mild alkali treatment (0.06 M-NaOH, room temperature, 5 min) releasing free [14C]galacturonic acid. The galacturonide appeared to be a single compound with one negative charge, as judged by TLC, paper electrophoresis and chromotography, LH-20 gel filtration and DEAE-cellulose column chromatography. Competition experiments indicated that the true glycosyl donor was UDP-GalA, in agreement with the detection of UDP-GlcA-4-epimerase activity in the crude enzyme preparation. The transglycosidase activity was located mainly in the membrane fraction. UDP inhibited the reaction and even produced some loss of label, suggesting an easily reversible reaction. UMP had almost no effect.
author	Baldessari, Alicia Ielpi, Luis Dankert, Marcelo Alberto
author_facet	Baldessari, Alicia Ielpi, Luis Dankert, Marcelo Alberto
author_sort	Baldessari, Alicia
title	A novel galacturonide from Xanthomonas campestris
title_short	A novel galacturonide from Xanthomonas campestris
title_full	A novel galacturonide from Xanthomonas campestris
title_fullStr	A novel galacturonide from Xanthomonas campestris
title_full_unstemmed	A novel galacturonide from Xanthomonas campestris
title_sort	novel galacturonide from xanthomonas campestris
publishDate	1990
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221287_v136_n8_p1501_Baldessari http://hdl.handle.net/20.500.12110/paper_00221287_v136_n8_p1501_Baldessari
work_keys_str_mv	AT baldessarialicia anovelgalacturonidefromxanthomonascampestris AT ielpiluis anovelgalacturonidefromxanthomonascampestris AT dankertmarceloalberto anovelgalacturonidefromxanthomonascampestris AT baldessarialicia novelgalacturonidefromxanthomonascampestris AT ielpiluis novelgalacturonidefromxanthomonascampestris AT dankertmarceloalberto novelgalacturonidefromxanthomonascampestris
_version_	1840321013166899200

A novel galacturonide from Xanthomonas campestris

Ejemplares similares