Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Rikke Høegh Lorentsen"'
Autor:
L. F. Romero, Susan Lund Arent, S. P. Ndou, Jung Min Heo, C. M. Nyachoti, Elijah G. Kiarie, A. K. Agyekum, Rikke Høegh Lorentsen
Publikováno v:
Animal Feed Science and Technology. 209:230-239
Two experiments were conducted to determine the effects of supplemental xylanases on growth performance, coefficients of apparent ileal (CAID) and total tract (CATTD) digestibility in growing pigs fed wheat- or corn -based diets. Two basal diets were
Autor:
Mads Brogger Pedersen, Helle Nygaard Lærke, Shukun Yu, Knud Erik Bach Knudsen, Søren Dalsgaard, Susan Lund Arent, Rikke Høegh Lorentsen
Publikováno v:
Pedersen, M B, Dalsgaard, S, Arent, S, Lorentsen, R, Knudsen, K E B, Yu, S & Lærke, H N 2015, ' Xylanase and Protease Increase Solubilization of Non-Starch Polysaccharides and Nutrient Release of Corn-and Wheat Distillers Dried Grains with Solubles ', Biochemical Engineering Journal, vol. 98, pp. 99-106 . https://doi.org/10.1016/j.bej.2015.02.036
The use of distiller dried grains with solubles (DDGS) as alternative to conventional animal feed for non-ruminants is challenged by the high content of non-starch polysaccharides and varying protein quality. In this study the enzymatic degradation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93fab054cea08f06261b4fe4995d5450
https://pure.au.dk/portal/da/publications/xylanase-and-protease-increase-solubilization-of-nonstarch-polysaccharides-and-nutrient-release-of-corn-and-wheat-distillers-dried-grains-with-solubles(6447a309-57f8-4f61-8d05-e85355a81fb2).html
https://pure.au.dk/portal/da/publications/xylanase-and-protease-increase-solubilization-of-nonstarch-polysaccharides-and-nutrient-release-of-corn-and-wheat-distillers-dried-grains-with-solubles(6447a309-57f8-4f61-8d05-e85355a81fb2).html
Autor:
Charlotte H. Møller, Hans Christian Thøgersen, Rikke Høegh Lorentsen, Thor Las Holtet, Michael Etzerodt
Publikováno v:
Org. Biomol. Chem.. 1:1657-1663
A library of blood coagulation factor Xa (FXa)–trypsin hybrid proteases was generated and displayed on phage for selection of derivatives with the domain “architecture” of trypsin and the specificity of FXa. Selection based on binding to soybea
Autor:
Jonas Heilskov Graversen, Søren K. Moestrup, Bent W. Sigurskjold, Rikke Høegh Lorentsen, Hans Christian Thøgersen, Christian Bøtcher Jacobsen, Michael Etzerodt
Publikováno v:
Journal of Biological Chemistry. 275:37390-37396
C-type lectin-like domains are found in many proteins, where they mediate binding to a wide diversity of compounds, including carbohydrates, lipids, and proteins. The binding of a C-type lectin-like domain to a ligand is often influenced by calcium.
Autor:
Nigel R. Caterer, Rikke Høegh Lorentsen, Jonas Heilskov Graversen, Hans Christian Thøgersen, Michael Etzerodt
Publikováno v:
Biochemical Journal. 347:83-87
Tetranectin is a homotrimeric plasma and extracellular-matrix protein that binds plasminogen and complex sulphated polysaccharides including heparin. In terms of primary and tertiary structure, tetranectin is related to the collectin family of Ca2+-b
Autor:
Søren K. Moestrup, Michael Etzerodt, Jonas Heilskov Graversen, Christian Jacobsen, Hans Christian Thøgersen, Bent W. Sigurskjold, Rikke Høegh Lorentsen
Publikováno v:
Journal of Biological Chemistry. 273:29241-29246
Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interac
Autor:
Michael Etzerodt, Thor Las Holtet, Rikke Høegh Lorentsen, Charlotte Harkjaer Fynbo, Hans Christian Thøgersen
Publikováno v:
Protein expression and purification. 39(2)
Blood coagulation factor Xa (FXa) and Thrombin are well-known serine proteases often used for processing of recombinant fusion proteins, but because they are purified from bovine blood or other animal sources, there is a risk of pathogenic contaminan
Autor:
Charlotte Harkjaer Fynbo, Thor Las Holtet, Hans Christian Thøgersen, Michael Etzerodt, Rikke Høegh Lorentsen
Publikováno v:
Lorentsen, R H, Fynbo, C H, Thøgersen, H C, Etzerodt, M & Holtet, T L 2005, ' Expression, refolding and purification of recombinant human granzyme B ', Prot. Expr. Purif, vol. 39, no. 1, pp. 18-26 .
Granzyme B (GrB) is a member of a family of serine proteases involved in cytotoxic T-lymphocyte-mediated killing of potentially harmful cells, where GrB induces apoptosis by cleavage of a limited number of substrates. To investigate the suitability o