ArticleLipids in health and disease2011
Purification and biochemical characterization of a secreted group IIA chicken intestinal phospholipase A₂.
Article in Lipids in health and disease, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- Untargeted metabolomics reveals the alteration of metabolites during the stewing process of Lueyang black-bone chicken meat.Frontiers in nutrition · 2024Article
- Hydrolysis of three different head groups phospholipids by chicken group V phospholipase A2 using the monomolecular film technique.Bioscience reports · 2020Article
- DEPTOR at the Nexus of Cancer, Metabolism, and Immunity.Physiological reviews · 2018Review
- Article
- Drastic changes in the tissue-specific expression of secreted phospholipases A2 in chicken pulmonary disease.Biochimie · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSecretory phospholipase A2 group IIA (IIA PLA2) is a protein shown to be highly expressed in the intestine of mammals. However, no study was reported in birds.
resultsChicken intestinal group IIA phospholipase A₂ (ChPLA₂-IIA) was obtained after an acidic treatment (pH.3.0), precipitation by ammonium sulphate, followed by sequential column chromatographies on Sephadex G-50 and mono-S ion exchanger. The enzyme was found to be a monomeric protein with a molecular mass of around 14 kDa. The purified enzyme showed a substrate preference for phosphatidylethanolamine and phosphatidylglycerol, and didn't hydrolyse phosphatidylcholine. Under optimal assay conditions, in the presence of 10 mM NaTDC and 10 mM CaCl₂, a specific activity of 160 U.mg⁻¹ for purified ChPLA₂-IIA was measured using egg yolk as substrate. The fifteen NH2-terminal amino acid residues of ChPLA₂-IIA were sequenced and showed a close homology with known intestinal secreted phospholipases A₂. The gene encoding the mature ChPLA₂-IIA was cloned and sequenced. To further investigate structure-activity relationship, a 3D model of ChPLA₂-IIA was built using the human intestinal phospholipase A₂ structure as template.
conclusionChPLA2-IIA was purified to homogeneity using only two chromatographic colomns. Sequence analysis of the cloned cDNA indicates that the enzyme is highly basic with a pI of 9.0 and has a high degree of homology with mammalian intestinal PLA₂-IIA.
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