The matrix metalloproteinase pump-1 catalyzes formation of low molecular weight (pro)urokinase in cultures of normal human kidney cells

The enzyme responsible for the metalloproteinase activity which cleaves the Glu143-Leu144 bond of (pro)urokinase has been isolated from the conditioned medium of cultured normal human kidney cells. Using S-Sepharose and Cibacron Blue-agarose chromatography, then C-4 reversed phase high pressure liqu...

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Veröffentlicht in:	The Journal of biological chemistry 1992-07, Vol.267 (20), p.13803-13806
Hauptverfasser:	MARCOTTE, P. A, KOZAN, I. M, DORWIN, S. A, RYAN, J. M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences cells Cells, Cultured Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel enzymatic activity Enzyme Precursors - isolation & purification Enzyme Precursors - metabolism Enzymes and enzyme inhibitors formation Fundamental and applied biological sciences. Psychology Humans Hydrolases Kidney - enzymology man Matrix Metalloproteinase 7 Metalloendopeptidases - genetics Metalloendopeptidases - isolation & purification Metalloendopeptidases - metabolism metalloproteinase PUMP-1 Molecular Sequence Data Molecular Weight plasminogen activator precursors purification Urokinase-Type Plasminogen Activator - isolation & purification Urokinase-Type Plasminogen Activator - metabolism
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