Evidence map›Paper›PMID 40274713›Full record

ArticleMolecular biotechnology2026

The Role of Calcium Ions in Restoring Lipase Activity of Recombinant Human Lipoprotein Lipase Expressed in Bacteria.

Chong Lee Ng, Theam Soon Lim, Yee Siew Choong

Abstract read
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Article in Molecular biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Chong Lee NgInstitute for Research in Molecular Medicine (INFORMM), Universiti Sains Malaysia, 11800, Penang, Malaysia.
Theam Soon LimInstitute for Research in Molecular Medicine (INFORMM), Universiti Sains Malaysia, 11800, Penang, Malaysia.
Yee Siew ChoongInstitute for Research in Molecular Medicine (INFORMM), Universiti Sains Malaysia, 11800, Penang, Malaysia. yeesiew@usm.my.ORCID http://orcid.org/0000-0001-5067-2073

Funding

Universiti Sains Malaysia R501-LR-RND003-0000000972-0000
6 · The paper itself

Abstract

Lipoprotein lipase (LPL) is a blood vessel lipase that regulates and removes plasma lipoprotein triglycerides from blood circulation. It is important in the control of hypertriglyceridemia. LPL dysregulation can lead to hypertriglyceridemia and increase the risk of atherosclerosis cardiovascular disease. Therefore, the biochemical characterization of LPL could help understand the LPL dysregulation mechanism. However, active LPL enzyme acquisition via bacterial expression is challenging, as studies have reported that LPL could only be co-expressed in the presence of a chaperone. Therefore, this work intends to investigate the possibility of bacterial expression of human LPL (hLPL) with active lipase activity. The hLPL protein has been produced in SHuffle® T7 cells, and the optimal refolding conditions of the hLPL protein have been described here. The addition of 4% glycerol, 0.5-M NaCl, and 0.5-mM CaCl

Indexed as

CalciumLipoprotein LipaseEscherichia coliHumansKineticsProtein RefoldingRecombinant ProteinsCalciumLipoprotein LipaseLPL protein, humanRecombinant ProteinsAtherosclerosisLipase activityp-Nitrophenol butyrate assayRefolding active recombinant lipoprotein lipase

Identifiers

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Registered trials

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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.