Searched for: subject:"Protein%5C%2BBinding"
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Gaubius Instituut TNO (author), Sakharov, D.V. (author), Lijnen, H.R. (author), Rijken, D.C. (author)
Staphylokinase (STA), a protein of bacterial origin, induces highly fibrin-specific thrombolysis both in human plasma in vitro and in pilot clinical trials. Using fluorescence microscopy, we investigated the spatial distribution of fluorescein isothiocyanate (FITC)-labeled STA during lysis of a plasma clot and its binding to purified fibrin...
article 1996
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Smit, E. (author), Jager, D. (author), Martinez, B. (author), Tielen, F.J. (author), Pouwels, P.H. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
The structure of the crystallisation domain, SAN, of the S A-protein of Lactobacillus acidophilus ATCC 4356 was analysed by insertion and deletion mutagenesis, and by proteolytic treatment. Mutant S A-protein synthesised in Escherichia coli with 7-13 amino acid insertions near the N terminus or within regions of sequence variation in SAN (amino...
article 2002
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Arand, M. (author), Hallberg, B.M. (author), Zou, J. (author), Bergfors, T. (author), Oesch, F. (author), van der Werf, M.J. (author), de Bont, J.A.M. (author), Jones, T.A. (author), Mowbray, S.L. (author)
Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an α/β hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus...
article 2003