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Structure of the elastase ec 3.4.21.11 cathepsin g ec 3.4.21.20 inhibitor of the leech hirudo medicinalis


, : Structure of the elastase ec 3.4.21.11 cathepsin g ec 3.4.21.20 inhibitor of the leech hirudo medicinalis. Hoppe Seyler's Zeitschrift fuer Physiologische Chemie 361(12): 1841-1846

H. medicinalis contains 3 groups of proteinase inhibitor proteins: thrombin-specific hirudin; bdellins directed against trypsin [EC 3.4.21.4], plasmin and acrosin; and eglins. The eglins are studied for 2 reasons. They form strong complexes with the granulocytic elastase and cathepsin G, with Ki values close to 1 .times. 10-10 mol/l. Due to this property they are potential candidates for the therapeutic treatment of various diseases. 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 and to proteolytic degradation.

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