Hydrolysis of three different head groups phospholipids by chicken group V phospholipase A2 using the monomolecular film technique
| Autor: | Bezzine Sofiane, Jallouli Raida, Madiha Bou Ali, Aida Karray |
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| Rok vydání: | 2019 |
| Předmět: |
binding surface
Biophysics 030209 endocrinology & metabolism 030204 cardiovascular system & hematology Phospholipase Biochemistry 03 medical and health sciences chemistry.chemical_compound Hydrolysis 0302 clinical medicine Phospholipase A2 Phosphatidylcholine Animals lipid monolayer penetration capacity Molecular Biology Pancreas Phospholipids Research Articles chemistry.chemical_classification Phosphatidylglycerol Phosphatidylethanolamine Phospholipase A2 group V Chromatography biology Phosphatidylethanolamines Fatty Acids Fatty acid Substrate (chemistry) Cell Biology Intestines Kinetics Phospholipases A2 chemistry biology.protein Phosphatidylcholines Enzymology Chickens Biotechnology |
| Zdroj: | Bioscience Reports |
| ISSN: | 1573-4935 |
| Popis: | The kinetic aspects of lipolysis by pulmonary phospholipase A2 (ChPLA2-V), chicken intestinal phospholipase A2 (ChPLA2-IIA) and chicken pancreatic phospholipase A2 (ChPLA2-IB), from chicken have been compared using the monomolecular films technique, on short-chain phospholipids (with three different head groups) and on long-chain phospholipids. The main conclusions from our experimental data indicate that the maximum catalytic activities of ChPLA2-V on 1,2 phosphatidylcholine and 1,2 phosphatidylethanolamine reached 15.26 and 36.12 moles/cm2.min.mM, respectively, at a pressure of 15 and 35 dynes/cm, respectively. Whereas, those of ChPLA2-IB were 3.58 (at the pressure of 20 dynes/cm) and 4.9 moles/cm2.min.mM. However, hydrolysis of phosphatidylglycerol monolayers (C12PG), were very much higher compared with all the substrates tested with 122 moles/cm2.min. Surprisingly, the hydrolysis rate of ChPLA2-V on long-chain phosphatidylglycerol (C18PG) was very low (1.45 moles/cm2.min) compared with all tested substrates, even with the use of p-cyclodextrin. And thus, the fatty acid preference of ChPLA2-V was 2-decanoyl > 2-oleoyl with a PG head group. In order to gain significant correlations between enzyme’s structures and their relative functions, we tried to examine the surface electrostatic potentials of the various secreted phospholipase 2 (sPLA2) from chicken. In the present study, we detailed that the substrate affinity, specificity and the hydrolysis rates of sPLA2 at each interface is governed by the surface electrostatic potentials and hydrophobic interactions operative at this surface. |
| Databáze: | OpenAIRE |
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