ArticleJournal of lipid research2010
A gel-based method for purification of apolipoprotein A-I from small volumes of plasma.
Article in Journal of lipid research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Trial
- HDL-Chitosan Nanoparticles for siRNA Delivery as an SR-B1 Receptor Targeted System.Combinatorial chemistry & high throughput screening · 2023Article
- Effect of Lipid Composition on the Atheroprotective Properties of HDL-Mimicking Micelles.Pharmaceutics · 2022Article
- Affinity binding of chicken apolipoprotein A1 to a novel flax orbitide (linusorb).RSC advances · 2018Article
- A facile method for isolation of recombinant human apolipoprotein A-I from E. coli.Protein expression and purification · 2017Article
- Lipoprotein (a) upregulates ABCA1 in liver cells via scavenger receptor-B1 through its oxidized phospholipids.Journal of lipid research · 2015Article
- Pegylation of high-density lipoprotein decreases plasma clearance and enhances antiatherogenic activity.Circulation research · 2013Article
- Functional rescue of mutant ABCA1 proteins by sodium 4-phenylbutyrate.Journal of lipid research · 2013Article
- HIV-1 Nef mobilizes lipid rafts in macrophages through a pathway that competes with ABCA1-dependent cholesterol efflux.Journal of lipid research · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present here a gel-based method for rapid purification of apolipoprotein A-I (apoA-I) from small volumes of human plasma. After isolation of high density lipoprotein from plasma, the apoA-I protein was separated by electrophoresis and the apoA-I band excised from the gel. The apoA-I was then eluted from the gel strip, concentrated, and delipidated ready for use. The structure and function of the gel-purified apoA-I protein was compared against apoA-I purified by the traditional size-exclusion chromatography method. The α-helical content of the gel-purified apoA-I as determined by circular dichroism was similar to chromatography-purified apoA-I. The functional activity of gel-purified apoA-I, as determined by cholesterol efflux assays in primary human fibroblasts and RAW264.7 macrophages, was also comparable with chromatography-purified apoA-I. This method is a valid alternative for apoA-I purification with some advantages over traditional chromatography purification including a much reduced plasma volume requirement, less time and cost, and a higher percentage protein recovery. The method is particularly suitable for applications requiring the purification of apoA-I from multiple human or animal samples of interest.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.