Regulation of elastolysis of insoluble elastin by human leukocyte elastase: stimulation by lysine-rich ligands, anionic detergents, and ionic strength

The present studies further describe the electrostatic and nonelectrostatic nature of HL elastase-elastin interactions and provide evidence that lysine-rich ligands such as platelet factor 4 stimulate HL elastase primarily by binding to the elastin substrate, thereby increasing productive elastolysi...

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Veröffentlicht in:	Biochemistry (Easton) 1983-07, Vol.22 (15), p.3714-3720
Hauptverfasser:	Lonky, Stewart A, Wohl, Herbert
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Cytoplasmic Granules - enzymology Detergents - pharmacology Elastin - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Kinetics leukocyte elastase Ligaments Ligands Lysine man Neutrophils - enzymology Osmolar Concentration Pancreatic Elastase - blood platelet factor 4 Platelet Factor 4 - physiology
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Beschreibung
Zusammenfassung:	The present studies further describe the electrostatic and nonelectrostatic nature of HL elastase-elastin interactions and provide evidence that lysine-rich ligands such as platelet factor 4 stimulate HL elastase primarily by binding to the elastin substrate, thereby increasing productive elastolysis.
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi00284a027