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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Yamamoto M, Yamamoto I, Tanaka Y, Sugano M

Department of Chemistry, Kurume University School of Medicine, Japan.

Comp Biochem Physiol B. 1987;88(1):363-8. doi: 10.1016/0305-0491(87)90128-3.

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, Yamamoto I, Tanaka Y, Sugano M

Department of Chemistry, Kurume University School of Medicine, Japan.

Comp Biochem Physiol B. 1987;88(1):363-8. doi: 10.1016/0305-0491(87)90128-3.

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.