Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Birgit Christine Bønsager"'
Publikováno v:
Phytochemistry. 71:1650-1656
Enzymes involved in redox control are important during seed germination and seedling growth. Ascorbate–glutathione cycle enzymes in barley embryo extracts were monitored both by 2D-gel electrophoresis and activity measurements from 4 to 144 h post
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52fc8d978af99b115d677c4cddeab85b
https://doi.org/10.1016/j.phytochem.2010.06.024
https://doi.org/10.1016/j.phytochem.2010.06.024
Autor:
Morten T. Jensen, X. Robert, Birgit Christine Bønsager, Nathalie Juge, Birte Svensson, S. Tranier, Richard Haser, Jane Nøhr, Martin Willemoës, M. Abou Hachem, Nushin Aghajari, Birte Kramhøft, Sophie Bozonnet, Kenji Fukuda
Publikováno v:
Biocatalysis and Biotransformation. 24:83-93
α-Amylases are endo-acting retaining enzymes of glycoside hydrolase family 13 with a catalytic (β/α)8-domain containing an inserted loop referred to as domain B and a C-terminal anti-parallel β-sheet termed domain C. New insights integrate the ro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f109cb46262e2492ca3c9d80e21fd0c5
https://doi.org/10.1080/10242420500516163
https://doi.org/10.1080/10242420500516163
Autor:
Birgit Christine Bønsager, Peter Kresten Nielsen, Birte Svensson, Mette Prætorius-Ibba, Maher Abou Hachem, Kenji Fukuda
Publikováno v:
Journal of Biological Chemistry. 280:14855-14864
The barley alpha-amylase/subtilisin inhibitor (BASI) inhibits alpha-amylase 2 (AMY2) with subnanomolar affinity. The contribution of selected side chains of BASI to this high affinity is discerned in this study, and binding to other targets is invest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e515080842d85d41971d942077edc39
https://doi.org/10.1074/jbc.m412222200
https://doi.org/10.1074/jbc.m412222200
Autor:
Johanne Mørch Jensen, Birgit Christine Bønsager, Maher Abou Hachem, Birte Svensson, Malene Bech Vester-Christensen, Marie Sofie Møller, Hans Erik Mølager Christensen
Publikováno v:
Protein expression and purification. 79(2)
The limit dextrinase inhibitor (LDI) from barley seeds acts specifically on limit dextrinase (LD), an endogenous starch debranching enzyme. LDI is a 14 kDa hydrophobic protein containing four disulfide bonds and one unpaired thiol group previously fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::461b9a11a45dce76f8a47c0412e829d3
https://pubmed.ncbi.nlm.nih.gov/21539920
https://pubmed.ncbi.nlm.nih.gov/21539920
Autor:
Christine Finnie, Bent W. Sigurskjold, Birgit Christine Bønsager, Maher Abou Hachem, Birte Svensson, Martin Willemoës, Sophie Bozonnet, Samuel Tranier, Kenji Maeda, Haruhide Mori, Richard Haser, Xavier Robert, Per Hägglund, Morten M. Nielsen, Malene H. Jensen, Nushin Aghajari, Birte Kramhøft, Kenji Fukuda
Publikováno v:
Journal of applied Glycoscience
Journal of applied Glycoscience, 2006, 53 (2), pp.163-169. ⟨10.5458/jag.53.163⟩
Journal of applied Glycoscience, 2006, 53 (2), pp.163-169. ⟨10.5458/jag.53.163⟩
Barley α-amylase binds sugars at two sites on the enzyme surface in addition to the active site. Crystallography and site-directed mutagenesis highlight the importance of aromatic residues at these surface sites as demonstrated by Kd values determin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba00a735ff869de99907441ebda15a18
https://hal.archives-ouvertes.fr/hal-03094801
https://hal.archives-ouvertes.fr/hal-03094801
Autor:
Sophie Bozonnet, Birgit Christine Bønsager, Kramhoft, B., Mori, H., Maher Abou Hachem, Martin Willemoes, Jensen, M. T., Kenji Fukuda, Nielsen, P. K., Juge, N., Aghajari, N., Tranier, S., Robert, X., Haser, R., Birte Svensson
Publikováno v:
HAL
Technical University of Denmark Orbit
Biologia
Biologia, Springer Verlag, 2005, 60, pp.27-36
Technical University of Denmark Orbit
Biologia
Biologia, Springer Verlag, 2005, 60, pp.27-36
International audience; xxx
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::0c99f14ad1f386950b3a06c5ff24816c
https://hal.archives-ouvertes.fr/hal-00314599
https://hal.archives-ouvertes.fr/hal-00314599