Searched for: subject:"Protein%5C%2BBinding"
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Peeters, K.A.B.M. (author), Nordlee, J.A. (author), Penninks, A.H. (author), Chen, L. (author), Goodman, R.E. (author), Bruijnzeel-Koomen, C.A.F.M. (author), Hefle, S.L. (author), Taylor, S.L. (author), Knulst, A.C. (author), TNO Kwaliteit van Leven (author)
Background: Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized. Objectives: We sought to identify allergens associated with...
article 2007
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Myrup, B. (author), Rossing, P. (author), Jensen, T. (author), Gram, J. (author), Kluft, C. (author), Jespersen, J. (author), Gaubius instituut TNO (author)
Objective: To investigate protein concentration changes during venous occlusion of proteins with reported affinity for extracellular matrix (plasminogen activator inhibitor type 1, antithrombin III, fibronectin and von Willebrand factor) in comparison with proteins with no reported affinity (albumin, tissue-type plasminogen activator,...
article 1999
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Rijken, D.C. (author), Barrett-Bergshoeff, M.M. (author), Jie, A.F.H. (author), Criscuoli, M. (author), Sakharov, D.V. (author), Gaubius Instituut TNO (author)
Amediplase (K2tu-PA) is a hybrid plasminogen activator, consisting of the kringle 2 domain of alteplase and the protease domain of urokinase. The objective of this study was to determine the in vitro clot penetration of amediplase in relation to its fibrin binding and to compare the properties with those of alteplase. The clot lysis activity of...
article 2004