Rat platelet phospholipase A2. Kinetic characterization using the monomolecular film technique
| Autor: | Christian Gancet, Robert Verger, Stéphane Ransac, Gerard H. de Haas, Henk van den Bosch, A.J. Aarsman |
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| Rok vydání: | 1992 |
| Předmět: |
Blood Platelets
Swine Motion Pictures Surface pressure Biochemistry Chromatography Affinity Phospholipases A chemistry.chemical_compound Non-competitive inhibition Phospholipase A2 Phosphatidylcholine Animals Platelet Pancreas chemistry.chemical_classification Elapid Venoms biology Chemistry Substrate (chemistry) Phosphatidylglycerols Enzyme assay Rats Intestines Kinetics Phospholipases A2 Enzyme biology.protein Phosphatidylcholines Electrophoresis Polyacrylamide Gel |
| Zdroj: | European journal of biochemistry. 204(2) |
| ISSN: | 0014-2956 |
| Popis: | We have determined some kinetic parameters of rat platelet phospholipase A2, such as surface pressure dependency and substrate specificity, using the monomolecular film technique. We found that rat platelet phospholipase A2 is very specific for phospholipids having a negatively charged headgroup, no activity was detected when using zwitterionic phospholipids such as phosphatidylcholine. Furthermore, the interfacial pressure window which permits enzyme activity is very narrow as compared to pancreatic phospholipase A2. Maximal enzyme activity is found at 22 mN/m when using 1,2-dilauroylphosphatidylglycerol as substrate. Studies of the competitive inhibition of mixed films containing 2-acylaminophosphatidylglycol show that platelet phospholipase A2 is less sensitive than pancreatic and intestinal phospholipase A2. These results imply that, despite the high degree of sequence similarity, one must be very cautious in extrapolating inhibition data from one phospholipase A2 to similar enzymes from other origins. |
| Databáze: | OpenAIRE |
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