Novel method of purification of human leukocytic elastase using adsorption on a high-performance liquid chromatography gel permeation column.
Neutrophil elastases are serine proteinases released during acute and chronic inflammatory states. We have developed a novel isolation method for neutrophil elastase, involving conventional gel chromatography followed by adsorption of protein at low ionic strength on a high-performance liquid chromatography gel permeation column. The bound elastase is then eluted by application of higher ionic strength. This adsorption step at low ionic strength, a step to be avoided in most purification methods, was used to advantage here to allow isolation of homogeneous material. This purification procedure should be useful for quick, simple bulk preparation of the enzyme.
Department of Biochemistry, Rush-Presbyterian-St. Luke's Medical Center, Chicago, IL 60612.
K
K
Kang
D
D
Schwarz
H
H
Sky-Peck
K E
KE
Kuettner
G A
GA
Homandberg
D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D019272:Leukocyte Elastase; D010196:Pancreatic Elastase / Q000302:isolation & purification*; D013056:Spectrophotometry, Ultraviolet
D010196:Pancreatic Elastase; D019272:Leukocyte Elastase