Journal article
A purification method for apolipoprotein A-I and A-II.
- Peitsch MC Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
- Kress A
- Lerch PG
- Morgenthaler JJ
- Isliker H
- Heiniger HJ
- 1989-05-01
Published in:
- Analytical biochemistry. - 1989
Apolipoprotein A-I
Apolipoprotein A-II
Apolipoproteins A
Blotting, Western
Electrophoresis, Polyacrylamide Gel
Humans
Phosphatidylcholine-Sterol O-Acyltransferase
Ultracentrifugation
English
Apolipoproteins A-I and A-II were isolated from precipitates obtained by cold ethanol fractionation of human plasma. The starting material used in this report was precipitate B of the Kistler and Nitschmann method which corresponds approximately to fraction III of the Cohn and Oncley procedure. Through the use of urea, chloroform, and ethanol in appropriate concentrations, apolipoproteins A-I and A-II were isolated by a simple extraction technique avoiding time-consuming ultracentrifugation. Starting from 10 g of centrifuged precipitate B, approximately 100 mg of apolipoprotein A-I and 10 mg of apolipoprotein A-II were obtained. When incubated with normal human or rabbit plasma, both apolipoproteins were readily incorporated into high-density lipoproteins. Apolipoprotein A-I obtained by the cold ethanol method activated lecithin-cholesterol acyltransferase to the same extent as apolipoprotein A-I prepared by the classical flotation method. Apolipoprotein A-II had no such properties by itself, but was capable of potentiating lecithin-cholesterol acyltransferase activity of apolipoprotein A-I.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1016/0003-2697(89)90642-8
- PMID 2502043
- Persistent URL
- https://sonar.ch/global/documents/250836
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