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Literature DB >> 6562888

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

Abstract

The rate constants for the inhibition of human leucocyte elastase by eglin from the leech Hirudo medicinalis were determined by using a pre-steady-state kinetic approach. kon and koff for complex-formation and dissociation were 1 X 10(6)M-1 X S-1 and 8 X 10(-4)S-1 respectively. Ki was calculated as the ratio koff/kon = 8 X 10(-10)M, the binding of eglin to elastase was reversible and the inhibition mechanism was of the fully competitive type. The mechanistic properties of the system and the biological significance of the rate constants are discussed.

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Year: 1984 PMID： 6562888 PMCID： PMC1153411 DOI： 10.1042/bj2180829

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

14 in total

1. Pancreatic trypsin inhibitor. II. Reaction with trypsin.

Authors: N M GREEN; E WORK
Journal: Biochem J Date: 1953-05 Impact factor: 3.857

2. Evaluation of the protease-antiprotease theory of human destructive lung disease.

Authors: J E Gadek; G W Hunninghake; G A Fells; R L Zimmerman; B A Keogh; R G Crystal
Journal: Bull Eur Physiopathol Respir Date: 1980

Review 3. Protein inhibitors of proteinases.

Authors: M Laskowski; I Kato
Journal: Annu Rev Biochem Date: 1980 Impact factor: 23.643

4. Pathophysiological interpretation of kinetic constants of protease inhibitors.

Authors: J G Bieth
Journal: Bull Eur Physiopathol Respir Date: 1980

5. Tight-binding inhibitors--VII. Extended interpretation of the rate equation experimental designs and statistical methods.

Authors: S Cha
Journal: Biochem Pharmacol Date: 1980-06-15 Impact factor: 5.858

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

Authors: U Seemüller; M Eulitz; H Fritz; A Strobl
Journal: Hoppe Seylers Z Physiol Chem Date: 1980-12

7. The slow, tight-binding inhibition of cathepsin B by leupeptin. A hysteretic effect.

Authors: A Baici; M Gyger-Marazzi
Journal: Eur J Biochem Date: 1982-12

8. Inhibition of human elastase from polymorphonuclear leucocytes by gold sodium thiomalate and pentosan polysulfate (SP-54).

Authors: A Baici; P Salgam; K Fehr; A Böni
Journal: Biochem Pharmacol Date: 1981-04-01 Impact factor: 5.858

9. Cathepsin G from human polymorphonuclear leukocytes cleaves human IgM.

Authors: A Baici; M Knöpfel; K Fehr
Journal: Mol Immunol Date: 1982-05 Impact factor: 4.407

10. Clotting and other plasma factors in experimental endotoxemia: inhibition of degradation by exogenous proteinase inhibitors.

Authors: M Jochum; J Witte; H Schiessler; H K Selbmann; G Ruckdeschl; H Fritz
Journal: Eur Surg Res Date: 1981 Impact factor: 1.745

5 in total

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

1. Pancreatic trypsin inhibitor. II. Reaction with trypsin.

2. Evaluation of the protease-antiprotease theory of human destructive lung disease.

Review 3. Protein inhibitors of proteinases.

4. Pathophysiological interpretation of kinetic constants of protease inhibitors.

5. Tight-binding inhibitors--VII. Extended interpretation of the rate equation experimental designs and statistical methods.

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

7. The slow, tight-binding inhibition of cathepsin B by leupeptin. A hysteretic effect.

8. Inhibition of human elastase from polymorphonuclear leucocytes by gold sodium thiomalate and pentosan polysulfate (SP-54).

9. Cathepsin G from human polymorphonuclear leukocytes cleaves human IgM.

10. Clotting and other plasma factors in experimental endotoxemia: inhibition of degradation by exogenous proteinase inhibitors.

1. Tridegin, a new peptidic inhibitor of factor XIIIa, from the blood-sucking leech Haementeria ghilianii.

2. Kinetics of the inhibition of human pancreatic elastase by recombinant eglin c. Influence of elastin.

3. The inhibitory effects of antirheumatic drugs on the activity of human leukocyte elastase and cathepsin G.

4. Recombinant C1 inhibitor P5/P3 variants display resistance to catalytic inactivation by stimulated neutrophils.

5. Inhibition of human pancreatic proteinases by mucus proteinase inhibitor, eglin c and aprotinin.