STRUCTURE OF THE ELASTASE-CATHEPSIN-G INHIBITOR OF THE LEECH HIRUDO-MEDICINALIS
- 1 January 1980
- journal article
- research article
- Vol. 361 (12), 1841-1846
Abstract
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.This publication has 3 references indexed in Scilit:
- Human α1-Antitrypsin Characterization and N- and C-Terminal Sequences1The Journal of Biochemistry, 1978
- Isolation and Characterisation of a Low Molecular Weight Inhibitor (of Chymotrypsin and Human Granulocytic Elastase and Cathepsin G) from LeechesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Inhibition of Chymotrypsin Activity in Crystalline Trypsin PreparationsJournal of Biological Chemistry, 1964