Porcine pancreatic phospholipase A2 isoforms: differential regulation by heparin
| Autor: | Cleris M. Gil, Judith A.K. Harmony, Mitchell B. Diccianni, Meenakshi J. Mistry, William D. Stuart, Larry R. McLean |
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| Rok vydání: | 1991 |
| Předmět: |
Gene isoform
Protein Conformation Swine Molecular Sequence Data Biophysics chemistry.chemical_element macromolecular substances Calcium Biochemistry Peptide Mapping Chromatography Affinity Phospholipases A Endocrinology Phospholipase A2 stomatognathic system Affinity chromatography medicine Animals Amino Acid Sequence Pancreas chemistry.chemical_classification biology Chemistry Heparin Active site respiratory system Hydrogen-Ion Concentration equipment and supplies Peptide Fragments Isoenzymes Molecular Weight Phospholipases A2 Enzyme medicine.anatomical_structure biology.protein lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel medicine.drug |
| Zdroj: | Biochimica et biophysica acta. 1082(1) |
| ISSN: | 0006-3002 |
| Popis: | Isoforms of porcine pancreatic phospholipase A 2 (PLA 2 ) can be differentially regulated by heparin. The major isoform of PLA 2 can bind to heparin-Affigel and its catalytic activity can be inhibited by heparin. The interaction between this PLA 2 isoform and heparin does not require calcium ion or a functional active site. The sensitivity to heparin inhibition depends on the pH, with optimum sensitivity at pH 5–7 and greatly diminished sensitivity as the pH is increased from 7 to 10. A minor isoform of porcine pancreatic PLA 2 cannot bind to heparin and is resistant to heparin inhibition. The resistant isoform appears to be iso-pig PLA 2 . Heparin affinity chromatography therefore offers a convenient route to the isolation of structurally and functionally distinct classes of PLA 2 enzymes. The existence of classes of PLA 2 that can be differentially regulated by heparin may have important physiological consequences. |
| Databáze: | OpenAIRE |
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