Purification of horse (Equus caballus) serum lecithin:cholesterol acyltransferase.
1. A method for the purification of horse serum lecithin:cholesterol acyltransferase has been established. 2. The method involves the adsorption of the enzyme from diluted horse serum on DEAE-Sephadex A-50, (NH4)2SO4 fractionation, 1-butanol treatment, and chromatographic techniques of DEAE-Sepharose CL-6B, DEAE-Sephadex A-50, Affi-Gel blue and hydroxylapatite. 3. The resultant enzyme preparation essentially formed a single main band when subjected to polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. 4. The final purification of the enzyme was 20,000-fold with 7% yield. 5. The apparent mol. wt of the enzyme was 64,000. 6. The activity of the enzyme was stable for 3 days at 0 degree C.
Yamamoto
M
M
Department of Chemistry, Kurume University School of Medicine, Japan.
Yamamoto
I
I
Tanaka
Y
Y
Sugano
M
M
D000818:Animals; D002845:Chromatography; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange / Q000379:methods; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006736:Horses / Q000097:blood*; D006882:Hydroxyapatites; D007700:Kinetics; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000097:blood* / Q000302:isolation & purification
D006882:Hydroxyapatites; D017886:Durapatite; D007862:Phosphatidylcholine-Sterol O-Acyltransferase