[Isolation and various properties of immobilized cholesterol esterase].
Immobilization of cholesterol esterase enabled to study the enzymatic modification of blood serum lipoproteins during their interaction with cells. Due to high affinity of octyl-Sepharose to cholesterol esterase large volumes of diluted enzyme preparations were immobilized without preliminary concentration. After immobilization the enzyme pH optimum was unaltered, whereas the activating effect of low NaCl concentrations and inhibitory effect of the salt high concentrations were not observed. The immobilized on octyl-Sepharose cholesterol esterase exhibited the greater stability as compared with the enzyme diluted preparation and was used repeatedly without distinct decrease in activity.
Kovaleva
G G
GG
Karmanskiĭ
I M
IM
D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000032:analysis / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D019301:Oleic Acid; D009829:Oleic Acids / Q000378:metabolism; D012685:Sepharose / Q000031:analogs & derivatives; D012995:Solubility; D002787:Sterol Esterase / Q000032:analysis / Q000302:isolation & purification*
D004800:Enzymes, Immobilized; D009829:Oleic Acids; D019301:Oleic Acid; C027176:octyl-sepharose CL-4B; D012685:Sepharose; D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase
Poluchenie i nekotorye svoĭstva immobilizovannoĭ kholesterolésterazy.