Searched for: subject:"Protein%5C%2BBinding"
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van Ruijven-Vermeer, I.A.M. (author), Nieuwenhuizen, W. (author), Nooijen, W.J. (author), Gaubius instituut TNO (author)
The authors studied the binding of Ca to rat fibrinogen and plasmic fibrin(ogen) degradation products by means of equilibrium dialysis with special reference to the protective effect of Ca2+ in the plasmic degradation of fibrinogen. Direct binding studies demonstrate that rat fibrinogen and the plasmic degradation products D(cate) and D-dimer...
article 1978
Nieuwenhuizen, W. (author), Voskuilen, M. (author), Hermans, J. (author), Gaubius instituut TNO (author)
The present study was undertaken as a step to delineate further the localization of the calcium-binding sites in fibrinogen and to assess the anticlotting properties of fibrinogen degradation products. To this purpose, fragments Y were prepared by plasmin digestion of human fibrinogen in the presence of added Ca2+, and purified. We found that,...
article 1982
Nieuwenhuizen, W.F. (author), Dekker, H.L. (author), Gröneveld, T. (author), de Koster, C.G. (author), de Jong, G.A.H. (author), TNO Voeding (author)
Bovine β-lactoglobulin (BLG) is a major component in whey and its physical properties are important for the texture of many dairy-based foods. Modification of proteins with transglutaminase from Streptoverticillium mobaraense (MTGase) can be used to alter their physical properties. MTGase-mediated modification of native BLG was until now,...
article 2004