[Purification of gelatinase secreted by human polynuclear neutrophils].
Gelatinase was purified from DFP treated human neutrophils which have been stimulated by the chemotactic peptide, N-formyl-methionyl-leucylphenylalanine. The secreted gelatinase was purified in two major steps: a gelatinase enriched fraction was recovered after a specific immunoadsorption of contaminant proteins from cytosol and immunoadsorption of proteins from specific or azurophilic granules; then gelatinase was isolated by affinity chromatography and FPLC gel filtration. Some kinetic properties of the Mr 94,000 purified enzyme were investigated.
Morel
F
F
Laboratoire d'Enzymologie, CHRU Grenoble.
Didier
F
F
Berthier
S
S
Dewald
B
B
D002384:Catalysis; D002623:Chemistry Techniques, Analytical / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D005780:Gelatin; D018093:Gelatinases; D006801:Humans; D009504:Neutrophils / Q000201:enzymology*; D010434:Pepsin A / Q000302:isolation & purification* / Q000378:metabolism
D005780:Gelatin; D010434:Pepsin A; D018093:Gelatinases
Purification de la gélatinase secrétée par les polynucléaires neutrophiles humains.