Literature DB >> 6906312

Structure of the elastase-cathepsin G inhibitor of the leech Hirudo medicinalis.

U Seemüller, M Eulitz, H Fritz, A Strobl.   

Abstract

The leech Hirudo medicinalis contains three different groups of proteinase inhibitor proteins, the thrombin-specific hirudin, the bdellins directed against trypsin, plasmin and acrosin, and the eglins which were discovered only recently. We are interested in the eglins mainly for two reasons: (i) They form strong complexes with the granulocytic elastase and cathepsin G with Ki values close to 1 x 10(-10) mol/l. Due to this property they are potential candidates for the therapeutic treatment of various diseases. (ii) Although the eglins do not contain a disulfide bridge to stabilize the tertiary structure, they are highly resistant to denaturation by acidification and by heat as well as to proteolytic degradation.

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Year:  1980        PMID： 6906312

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN： 0018-4888


  14 in total

Review 1.  Small bite, large impact-saliva and salivary molecules in the medicinal leech, Hirudo medicinalis.

Authors:  Jan-Peter Hildebrandt; Sarah Lemke
Journal:  Naturwissenschaften       Date:  2011-11-09

2.  Molecular characterization of a wound-inducible inhibitor I gene from potato and the processing of its mRNA and protein.

Authors:  T E Cleveland; R W Thornburg; C A Ryan
Journal:  Plant Mol Biol       Date:  1987-05       Impact factor: 4.076

3.  Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop.

Authors:  L L Beuning; T W Spriggs; J T Christeller
Journal:  J Mol Evol       Date:  1994-12       Impact factor: 2.395

4.  The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2.

Authors:  G J Martens; J A Braks; D W Eib; Y Zhou; I Lindberg
Journal:  Proc Natl Acad Sci U S A       Date:  1994-06-21       Impact factor: 11.205

5.  A large fragment approach to DNA synthesis: total synthesis of a gene for the protease inhibitor eglin c from the leech Hirudo medicinalis and its expression in E. coli.

Authors:  H Rink; M Liersch; P Sieber; F Meyer
Journal:  Nucleic Acids Res       Date:  1984-08-24       Impact factor: 16.971

6.  Kinetics of the inhibition of human leucocyte elastase by eglin from the leech Hirudo medicinalis.

Authors:  A Baici; U Seemüller
Journal:  Biochem J       Date:  1984-03-15       Impact factor: 3.857

7.  Protease inhibitors in the alimentary tract of the medicinal leech Hirudo medicinalis: in vivo and in vitro studies.

Authors:  F J Roters; E Zebe
Journal:  J Comp Physiol B       Date:  1992       Impact factor: 2.200

8.  A complete separation of dimethylaminoazobenzenesulphonyl-amino acids. Amino acid analysis with low nanogram amounts of polypeptide with dimethylaminoazobenzenesulphonyl chloride.

Authors:  J Y Chang; R Knecht; D G Braun
Journal:  Biochem J       Date:  1982-06-01       Impact factor: 3.857

9.  Molecular characterization and phylogenetic studies of a wound-inducible proteinase inhibitor I gene in Lycopersicon species.

Authors:  J S Lee; W E Brown; J S Graham; G Pearce; E A Fox; T W Dreher; K G Ahern; G D Pearson; C A Ryan
Journal:  Proc Natl Acad Sci U S A       Date:  1986-10       Impact factor: 11.205

10.  The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures.

Authors:  S G Hyberts; M S Goldberg; T F Havel; G Wagner
Journal:  Protein Sci       Date:  1992-06       Impact factor: 6.725
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