The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.)
Autor(a) principal: | |
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Data de Publicação: | 1997 |
Outros Autores: | , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10316/8137 https://doi.org/10.1111/j.1432-1033.1997.t01-1-00695.x |
Resumo: | Plant aspartic proteinases characterised at the molecular level contain one or more consensus N-glycosylation sites [Runeberg-Roos, P., Törmäkangas, K. & Östman, A. (1991) Eur. J. Biochem. 202, 102120131027; Asakura, T., Watanabe, H., Abe, K. & Arai, S. (1995) Eur. J. Biochem. 232, 77201383; Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J. & Pires, E. (1996) Eur. J. Biochem. 235, 76220137681. We found that the glycosylation sites are occupied for the barley (Hordeum vulgare L.) aspartic proteinase (Asn333) and the cardoon (Cynara cardunculus L.) aspartic proteinase, cardosin A (Asn70 and Asn363). The oligosaccharides from each site were released from peptide pools by enzymatic hydrolysis with peptide-N-glycanase A or by hydrazinolysis and their structures were determined by exoglycosidase sequencing combined with matrix-assisted laser desorption/ionization time of flight mass spectrometry. It was observed that 6% of the oligosaccharides from the first glycosylation site of cardosin A are of the oligomannose type. Modified type glycans with proximal Fuc and without Xyl account for about 82%, 14% and 3% of the total oligosaccharides from the first and the second glycosylation sites of cardosin A and from H. vulgare aspartic proteinase, respectively. Oligosaccharides with Xyl but without proximal Fuc were only detected in the latter proteinase (4%). Glycans with proximal Fuc and Xyl account for 6%, 86% and 92% of the total oligosaccharides from the first and second glycosylation sites of cardosin A and from H. vulgure aspartic proteinase, respectively. |
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The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.)Plant aspartic proteinases characterised at the molecular level contain one or more consensus N-glycosylation sites [Runeberg-Roos, P., Törmäkangas, K. & Östman, A. (1991) Eur. J. Biochem. 202, 102120131027; Asakura, T., Watanabe, H., Abe, K. & Arai, S. (1995) Eur. J. Biochem. 232, 77201383; Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J. & Pires, E. (1996) Eur. J. Biochem. 235, 76220137681. We found that the glycosylation sites are occupied for the barley (Hordeum vulgare L.) aspartic proteinase (Asn333) and the cardoon (Cynara cardunculus L.) aspartic proteinase, cardosin A (Asn70 and Asn363). The oligosaccharides from each site were released from peptide pools by enzymatic hydrolysis with peptide-N-glycanase A or by hydrazinolysis and their structures were determined by exoglycosidase sequencing combined with matrix-assisted laser desorption/ionization time of flight mass spectrometry. It was observed that 6% of the oligosaccharides from the first glycosylation site of cardosin A are of the oligomannose type. Modified type glycans with proximal Fuc and without Xyl account for about 82%, 14% and 3% of the total oligosaccharides from the first and the second glycosylation sites of cardosin A and from H. vulgare aspartic proteinase, respectively. Oligosaccharides with Xyl but without proximal Fuc were only detected in the latter proteinase (4%). Glycans with proximal Fuc and Xyl account for 6%, 86% and 92% of the total oligosaccharides from the first and second glycosylation sites of cardosin A and from H. vulgure aspartic proteinase, respectively.1997info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/8137http://hdl.handle.net/10316/8137https://doi.org/10.1111/j.1432-1033.1997.t01-1-00695.xengEuropean Journal of Biochemistry. 243:3 (1997) 695-700Costa, JúliaAshford, David A.Nimtz, ManfredBento, IsabelFrazão, CarlosEsteves, Cristina L.Faro, Carlos J.Kervinen, JukkaPires, EuclidesVeríssimo, PaulaWlodawer, AlexanderCarrondo, Maria Arméniainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2021-11-09T09:29:41Zoai:estudogeral.uc.pt:10316/8137Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:55:55.110561Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
title |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
spellingShingle |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) Costa, Júlia |
title_short |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
title_full |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
title_fullStr |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
title_full_unstemmed |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
title_sort |
The Glycosylation of the Aspartic Proteinases from Barley (Hordeum Vulgare L.) and Cardoon (Cynara Cardunculus L.) |
author |
Costa, Júlia |
author_facet |
Costa, Júlia Ashford, David A. Nimtz, Manfred Bento, Isabel Frazão, Carlos Esteves, Cristina L. Faro, Carlos J. Kervinen, Jukka Pires, Euclides Veríssimo, Paula Wlodawer, Alexander Carrondo, Maria Arménia |
author_role |
author |
author2 |
Ashford, David A. Nimtz, Manfred Bento, Isabel Frazão, Carlos Esteves, Cristina L. Faro, Carlos J. Kervinen, Jukka Pires, Euclides Veríssimo, Paula Wlodawer, Alexander Carrondo, Maria Arménia |
author2_role |
author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Costa, Júlia Ashford, David A. Nimtz, Manfred Bento, Isabel Frazão, Carlos Esteves, Cristina L. Faro, Carlos J. Kervinen, Jukka Pires, Euclides Veríssimo, Paula Wlodawer, Alexander Carrondo, Maria Arménia |
description |
Plant aspartic proteinases characterised at the molecular level contain one or more consensus N-glycosylation sites [Runeberg-Roos, P., Törmäkangas, K. & Östman, A. (1991) Eur. J. Biochem. 202, 102120131027; Asakura, T., Watanabe, H., Abe, K. & Arai, S. (1995) Eur. J. Biochem. 232, 77201383; Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J. & Pires, E. (1996) Eur. J. Biochem. 235, 76220137681. We found that the glycosylation sites are occupied for the barley (Hordeum vulgare L.) aspartic proteinase (Asn333) and the cardoon (Cynara cardunculus L.) aspartic proteinase, cardosin A (Asn70 and Asn363). The oligosaccharides from each site were released from peptide pools by enzymatic hydrolysis with peptide-N-glycanase A or by hydrazinolysis and their structures were determined by exoglycosidase sequencing combined with matrix-assisted laser desorption/ionization time of flight mass spectrometry. It was observed that 6% of the oligosaccharides from the first glycosylation site of cardosin A are of the oligomannose type. Modified type glycans with proximal Fuc and without Xyl account for about 82%, 14% and 3% of the total oligosaccharides from the first and the second glycosylation sites of cardosin A and from H. vulgare aspartic proteinase, respectively. Oligosaccharides with Xyl but without proximal Fuc were only detected in the latter proteinase (4%). Glycans with proximal Fuc and Xyl account for 6%, 86% and 92% of the total oligosaccharides from the first and second glycosylation sites of cardosin A and from H. vulgure aspartic proteinase, respectively. |
publishDate |
1997 |
dc.date.none.fl_str_mv |
1997 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10316/8137 http://hdl.handle.net/10316/8137 https://doi.org/10.1111/j.1432-1033.1997.t01-1-00695.x |
url |
http://hdl.handle.net/10316/8137 https://doi.org/10.1111/j.1432-1033.1997.t01-1-00695.x |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
European Journal of Biochemistry. 243:3 (1997) 695-700 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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