Use of anion-exchange high-performance liquid chromatography for the study of smooth muscle myosin light-chain kinase and its catalytic domain.
Avian myosin light-chain kinase from smooth muscle of the gizzard and its catalytic domain, derived from the intact enzyme by trypsin digestion, was purified within 30-40 min by both analytical and preparative anion-exchange high-performance liquid chromatography. The proteins obtained were more than 95% pure and retained their biological activity. The high-performance anion-exchange chromatography protocols represent a significant decrease in purification time when compared with conventional ion-exchange chromatography.
National Research Council Unit for Muscle Biology and Physiopathology, Institute of General Pathology, Italy.
L
L
Dalla Libera
M
M
Fasolo
P
P
Cavallini
E
E
Ratti
G
G
Gaviraghi
D000818:Animals; D000837:Anion Exchange Resins; D001665:Binding Sites; D002645:Chickens; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange; D005895:Gizzard, Avian / Q000201:enzymology; D009130:Muscle, Smooth / Q000201:enzymology*; D009219:Myosin-Light-Chain Kinase / Q000302:isolation & purification*; D012965:Sodium Chloride; D014422:Turkeys
D000837:Anion Exchange Resins; D012965:Sodium Chloride; D009219:Myosin-Light-Chain Kinase