Rat platelet phospholipase A2 : kinetic characterization using the monomolecular film technique
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...
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Veröffentlicht in: | European journal of biochemistry 1992-03, Vol.204 (2), p.793-797 |
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creator | RANSAC, S AARSMAN, A. J VAN DEN BOSCH, H GANCET, C DE HAAS, G. H VERGER, R |
description | 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. |
doi_str_mv | 10.1111/j.1432-1033.1992.tb16697.x |
format | Article |
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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.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1992.tb16697.x</identifier><identifier>PMID: 1541292</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford: Blackwell</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Blood Platelets - enzymology ; Chromatography, Affinity ; Elapid Venoms - enzymology ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrolases ; Intestines - enzymology ; Kinetics ; Motion Pictures ; Pancreas - enzymology ; Phosphatidylcholines - pharmacology ; Phosphatidylglycerols - pharmacology ; Phospholipases A - antagonists & inhibitors ; Phospholipases A - metabolism ; Phospholipases A2 ; Rats ; Swine</subject><ispartof>European journal of biochemistry, 1992-03, Vol.204 (2), p.793-797</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5284359$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1541292$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RANSAC, S</creatorcontrib><creatorcontrib>AARSMAN, A. J</creatorcontrib><creatorcontrib>VAN DEN BOSCH, H</creatorcontrib><creatorcontrib>GANCET, C</creatorcontrib><creatorcontrib>DE HAAS, G. H</creatorcontrib><creatorcontrib>VERGER, R</creatorcontrib><title>Rat platelet phospholipase A2 : kinetic characterization using the monomolecular film technique</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>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.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood Platelets - enzymology</subject><subject>Chromatography, Affinity</subject><subject>Elapid Venoms - enzymology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolases</subject><subject>Intestines - enzymology</subject><subject>Kinetics</subject><subject>Motion Pictures</subject><subject>Pancreas - enzymology</subject><subject>Phosphatidylcholines - pharmacology</subject><subject>Phosphatidylglycerols - pharmacology</subject><subject>Phospholipases A - antagonists & inhibitors</subject><subject>Phospholipases A - metabolism</subject><subject>Phospholipases A2</subject><subject>Rats</subject><subject>Swine</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kNtKxEAMQAdR1nX1E4RBxLfWuXXa-rYs3mBBEH0u6TS1s04vdqagfr0Flw2EhJxDAiHkirOYz3G7i7mSIuJMypjnuYhDybXO0_j7iCwP6JgsGeMqEnmiT8mZ9zvGmM51uiALnigucrEkxSsEOjgI6HBumt7P6ewAHula0Dv6aTsM1lDTwAgm4Gh_Idi-o5O33QcNDdK27_q2d2gmByOtrWtpQNN09mvCc3JSg_N4sa8r8v5w_7Z5irYvj8-b9TYahExClKkqqTJRCVlqlUJZlUKlKco0wTLTDJVIKzCSI2oxDxIGSqkSWcnrTBuo5Irc_O8dxn4-60PRWm_QOeiwn3yRikxkTItZvNyLU9liVQyjbWH8KfYfmfn1noM34OoROmP9QUtEpmSSyz_lLnN5</recordid><startdate>19920301</startdate><enddate>19920301</enddate><creator>RANSAC, S</creator><creator>AARSMAN, A. 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H ; VERGER, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p235t-84d5d82d23b647abdb2477e375eb860e427dac31ee62b8650a444be0b1f86cad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood Platelets - enzymology</topic><topic>Chromatography, Affinity</topic><topic>Elapid Venoms - enzymology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrolases</topic><topic>Intestines - enzymology</topic><topic>Kinetics</topic><topic>Motion Pictures</topic><topic>Pancreas - enzymology</topic><topic>Phosphatidylcholines - pharmacology</topic><topic>Phosphatidylglycerols - pharmacology</topic><topic>Phospholipases A - antagonists & inhibitors</topic><topic>Phospholipases A - metabolism</topic><topic>Phospholipases A2</topic><topic>Rats</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RANSAC, S</creatorcontrib><creatorcontrib>AARSMAN, A. J</creatorcontrib><creatorcontrib>VAN DEN BOSCH, H</creatorcontrib><creatorcontrib>GANCET, C</creatorcontrib><creatorcontrib>DE HAAS, G. H</creatorcontrib><creatorcontrib>VERGER, R</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RANSAC, S</au><au>AARSMAN, A. J</au><au>VAN DEN BOSCH, H</au><au>GANCET, C</au><au>DE HAAS, G. H</au><au>VERGER, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rat platelet phospholipase A2 : kinetic characterization using the monomolecular film technique</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1992-03-01</date><risdate>1992</risdate><volume>204</volume><issue>2</issue><spage>793</spage><epage>797</epage><pages>793-797</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>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.</abstract><cop>Oxford</cop><pub>Blackwell</pub><pmid>1541292</pmid><doi>10.1111/j.1432-1033.1992.tb16697.x</doi><tpages>5</tpages></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blood Platelets - enzymology Chromatography, Affinity Elapid Venoms - enzymology Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Intestines - enzymology Kinetics Motion Pictures Pancreas - enzymology Phosphatidylcholines - pharmacology Phosphatidylglycerols - pharmacology Phospholipases A - antagonists & inhibitors Phospholipases A - metabolism Phospholipases A2 Rats Swine |
title | Rat platelet phospholipase A2 : kinetic characterization using the monomolecular film technique |
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