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

article





Weening-Verhoeff, E.J.D.

Quax, P.H.A.

Leeuwen, R.T.J. van

Rehberg, E.F.

Marotti, K.R.

Verheijen, J.H.
Topics

















Chemical modificationLigand bindingSite directed mutagenesisAmino Acid SequenceAspartic AcidBase SequenceEthyldimethylaminopropyl CarbodiimideFibrinGlutamatesKineticsLysineMolecular Sequence DataMutagenesis, Site-DirectedMutationPeptide FragmentsPlasminogenProtein EngineeringTissue Plasminogen Activator
TNO Identifier
231340
Repository link
https://resolver.tno.nl/uuid:7558c259-ac80-4b78-8a72-d316e01af27b
ISSN
02692139
Source
Protein Engineering, 4(2), pp. 191-198.
Pages
191-198
Files
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