期刊论文详细信息
FEBS Letters
Interaction of site specific hirudin variants with α‐thrombin
Baici, Antonio1  Dodt, Johannes2  Köhler, Stefanie2 
[1] Forschungslabor der Rheumaklinik, Universitätsspital, Gloriastr. 25, CH-8091 Zürich, Switzerland;Institut für Biochemie der Technischen Hochschule Darmstadt, Petersenstr. 22, D-6100 Darmstadt, FRG
关键词: Hirudin;    Hirudin variant;    Site-directed mutagenesis;    Kinetics;    α-Thrombin;    Putative reactive site;    HPLC;    high-performance liquid chromatography;    IPTG;    isopropyl-β-D-thiogalactopyranoside;    RP;    reversed-phase;    Tos;    4-toluoslsulfonyl;   
DOI  :  10.1016/0014-5793(88)80803-2
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

The kinetics of complex formation between recombinant hirudin or recombinant hirudin mutants with thrombin were analyzed. In order to elucidate the inhibitor's reactive site peptide bond predetermined amino acid substitutions were introduced at positions of basic amino acid residues by means of site-directed mutagenesis of a hirudin gene. In comparison to recombinant hirudin (K i = 19 pM) only those mutant inhibitors which were modified at amino acid position Lys47 showed a higher K i value for their complexes with thrombin. The observed effects are mainly due to increased k off rate constants.

【 授权许可】

Unknown   

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