Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin

• Published in: Biochemistry (Easton) Vol. 32; no. 7; pp. 1866 - 1874
• Main Authors: Ying, Qi Long, Simon, Sanford R
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.02.1993
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Binding Sites; Binding, Competitive; Biological and medical sciences; Cytoplasmic Granules - enzymology; elafin; enzymatic activity; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humans; Hydrogen-Ion Concentration; Hydrolases; inhibition; Kinetics; Leukocyte Elastase; man; Molecular Sequence Data; Molecular Weight; Pancreatic Elastase - antagonists & inhibitors; Pancreatic Elastase - metabolism; Proteinase Inhibitory Proteins, Secretory; Proteins; Serine Proteinase Inhibitors - chemistry; Serine Proteinase Inhibitors - metabolism; Serine Proteinase Inhibitors - pharmacology; Skin - chemistry; Human; Enzymatic activity; Radiolabelling; Enzyme; Leukocyte; Analytical method; Enzyme inhibitor; Elastase; Kinetics; Substrate enzyme complex

We have investigated the kinetics of inhibition of human leukocyte elastase by elafin, a small protein originally isolated from human skin. A single inhibitor molecule was found to bind to a single site on the protease, blocking the reactive serine at the enzyme's catalytic center. Association...