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Involvement of aspartic and glutamic residues in kringle-2 of tissue-type plasminogen activator in lysine binding, fibrin binding and stimulation of activity as revealed by chemical modification and oligonucleotide-directed mutagenesis

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Author: Weening-Verhoeff, E.J.D. · Quax, P.H.A. · Leeuwen, R.T.J. van · Rehberg, E.F. · Marotti, K.R. · Verheijen, J.H.
Type:article
Date:1990
Institution: Gaubius Instituut TNO
Source:Protein Engineering, 2, 4, 191-198
Identifier: 231340
Keywords: Health · Chemical modification · Ligand binding · Site directed mutagenesis · Amino Acid Sequence · Aspartic Acid · Base Sequence · Ethyldimethylaminopropyl Carbodiimide · Fibrin · Glutamates · Kinetics · Lysine · Molecular Sequence Data · Mutagenesis, Site-Directed · Mutation · Peptide Fragments · Plasminogen · Protein Engineering · Tissue Plasminogen Activator