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|Title:||Electroelution of lipoprotein(a) [Lp(a)] from native polyacrylamide gels: A new, simple method to purify Lp(a)|
Lttan, P. S. Appukuttan
|Publisher:||JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS|
|Citation:||JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS. 68; 1; 43-53|
|Abstract:||Lipoprotein(a), Lp(a), is an atherogenic lipoprotein consisting of an LDL like core particle and a covalently linked glycoprotein of variable size. Lp(a). isolated front serum always contains LDL and HDL, as contaminants since Lp(a) floats in the density range 1.05-1.12 g/ml which overlaps that of LDL and HDL, Purified Lp(a) is increasingly needed as a standard to overcome various problems in the standardization of Lp(a) measurements and for in vitro biological studies. Problems inherent to the purification of Lp(a) include the aggregation of Lp(a) with LDL, overlapping size distribution and the inability of some fractions to bind to affinity columns. Here. we describe the development of a new method to purify Lp(a) from contaminating LDL and HDL, particles. Lp(a) was isolated from serurn by sequential ultracentrifugation, resolved by native polyacrylamide eel electrophoresis and the eel segments were electroeluted to obtain pure Lp(a). L-Proline was added to the sample to a final concentration of 0.1 M to prevent the aggregation of Lp(a) with LDL. (c) 2006 Elsevier B.V. All rights reserved.|
|Appears in Collections:||Journal Articles|
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