Searched for: subject%3A%22Cyanogen%255C%2BBromide%22
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Gaubius Instituut TNO (author), Bakker, A.H.F. (author), van der Greef, W. (author), Rehberg, E.F. (author), Marotti, K.R. (author), Verheijen, J.H. (author)
Despite the high overall similarity in primary structure between kringle one (K1) and kringle two (K2) of tissue-type plasminogen activator (t-PA) there exists an enormous functional difference. It is thought that, in contrast to K1, K2 mediates lysine binding and fibrin binding and is involved in stimulation of plasminogen activation by fibrin...
article 1993
Instituut voor verouderings- en vaatziekten onderzoek TNO (author), Yonekawa, O. (author), Voskuilen, M. (author), Nieuwenhuizen, W. (author)
In previous publications [e.g. Voskuilen, Vermond, Veeneman, Van Boom, Klasen, Zegers and Nieuwenhuizen (1987) J. Biol. Chem. 262, 5944-5946] we have shown that fibrin(ogen) chain fragment Aα-(148-160) contains a site that contributes to the acceleration of Glu-plasminogen activation by tissue-type plasminogen activator (t-PA). In contrast with...
article 1992
TNO Gaubius Institute for Cardiovascular Research, 2313 AD Leiden, Netherlands (author), Rijken, D.C. (author), Groeneveld, E. (author)
Two-chain tissue-type plasminogen activator (t-PA), which consists of a heavy chain (M(r) ??? 38,000) and a light chain (M(r) ??? 31,000) connected by a disulfide bridge, was reduced with 2-mercaptoethanol and then air-reoxidized at a low protein concentration and carboxamidomethylated. The two chains were separated by means of zinc chelate...
article 1986