Mechanism of Inhibition of Hepatic Triglyceride Lipase from Human Postheparin Plasma by Apolipoproteins A-I and A-II
The present data describe the mechanism of the inhibitory effects of human plasma apolipoproteins A-I and A-II on hydrolysis of triglyceride catalyzed by hepatic triglyceride lipase using a substrate of triolein particles stabilized with gum arabic in vitro. The experimental data could well be descr...
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Veröffentlicht in: | Journal of biochemistry (Tokyo) 1982, Vol.92 (3), p.865-870 |
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container_title | Journal of biochemistry (Tokyo) |
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creator | KUBO, Masaharu MATSUZAWA, Yuji YOKOYAMA, Shinji TAJIMA, Shoji ISHIKAWA, Katsunori YAMAMOTO, Akira TARUI, Seiichiro |
description | The present data describe the mechanism of the inhibitory effects of human plasma apolipoproteins A-I and A-II on hydrolysis of triglyceride catalyzed by hepatic triglyceride lipase using a substrate of triolein particles stabilized with gum arabic in vitro. The experimental data could well be described by a model in which apolipoproteins bound to the surface of lipid substrate particles inhibited the enzyme reaction. The values of Km obtained were similar with or without inhibitors and the calculated saturation levels of apolipoprotein binding to the lipid were in good agreement with those obtained in independent binding experiments. |
doi_str_mv | 10.1093/oxfordjournals.jbchem.a134000 |
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The experimental data could well be described by a model in which apolipoproteins bound to the surface of lipid substrate particles inhibited the enzyme reaction. The values of Km obtained were similar with or without inhibitors and the calculated saturation levels of apolipoprotein binding to the lipid were in good agreement with those obtained in independent binding experiments.</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a134000</identifier><identifier>PMID: 6815170</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Adult ; Apolipoprotein A-I ; Apolipoprotein A-II ; Apolipoproteins - isolation & purification ; Apolipoproteins - pharmacology ; Chemical Phenomena ; Chemistry ; Heparin - pharmacology ; Humans ; Kinetics ; Lipase - antagonists & inhibitors ; Lipase - blood ; Liver - enzymology ; Male ; man ; plasma ; triacylglycerol lipase ; triglycerides</subject><ispartof>Journal of biochemistry (Tokyo), 1982, Vol.92 (3), p.865-870</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6815170$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KUBO, Masaharu</creatorcontrib><creatorcontrib>MATSUZAWA, Yuji</creatorcontrib><creatorcontrib>YOKOYAMA, Shinji</creatorcontrib><creatorcontrib>TAJIMA, Shoji</creatorcontrib><creatorcontrib>ISHIKAWA, Katsunori</creatorcontrib><creatorcontrib>YAMAMOTO, Akira</creatorcontrib><creatorcontrib>TARUI, Seiichiro</creatorcontrib><title>Mechanism of Inhibition of Hepatic Triglyceride Lipase from Human Postheparin Plasma by Apolipoproteins A-I and A-II</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The present data describe the mechanism of the inhibitory effects of human plasma apolipoproteins A-I and A-II on hydrolysis of triglyceride catalyzed by hepatic triglyceride lipase using a substrate of triolein particles stabilized with gum arabic in vitro. The experimental data could well be described by a model in which apolipoproteins bound to the surface of lipid substrate particles inhibited the enzyme reaction. The values of Km obtained were similar with or without inhibitors and the calculated saturation levels of apolipoprotein binding to the lipid were in good agreement with those obtained in independent binding experiments.</description><subject>Adult</subject><subject>Apolipoprotein A-I</subject><subject>Apolipoprotein A-II</subject><subject>Apolipoproteins - isolation & purification</subject><subject>Apolipoproteins - pharmacology</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Heparin - pharmacology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Lipase - antagonists & inhibitors</subject><subject>Lipase - blood</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>man</subject><subject>plasma</subject><subject>triacylglycerol lipase</subject><subject>triglycerides</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD9PwzAQxT2ASil8BCQvsKX4T2I3Y6mAVmqBoaCKJbokNnFJ4mAnUvvtSdWKlenu3fvp9O4QuqVkTEnM7-1OW5dvbedqKP14m2aFqsZAeUgIOUNDQhgNYhZuLtCl99uDZJwP0EBMaEQlGaJ2pbICauMrbDVe1IVJTWtsfVBz1UBrMrx25qvcZ8qZXOGlacArrJ2t8LyroMZv1rdFjzrT9yX4CnC6x9PGlqaxjbOtMrXH02CBoc4PdXGFznWfV12f6gi9Pz2uZ_Ng-fq8mE2XgWGCt0GWTyIicgCQOk0zrSIlpNK6nxJGMkEhJjQSMeOUpaC5JqnkIGMt8qg_VPIRujvu7VP8dMq3SWV8psoSamU7n8iQxTHh4l-QRhEn4YT34M0J7NJK5UnjTAVun5z-2fvB0Te-Vbs_G9x3IiSXUTLffCYfq4cXsaIsWfNfO2mL4w</recordid><startdate>1982</startdate><enddate>1982</enddate><creator>KUBO, Masaharu</creator><creator>MATSUZAWA, Yuji</creator><creator>YOKOYAMA, Shinji</creator><creator>TAJIMA, Shoji</creator><creator>ISHIKAWA, Katsunori</creator><creator>YAMAMOTO, Akira</creator><creator>TARUI, Seiichiro</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>1982</creationdate><title>Mechanism of Inhibition of Hepatic Triglyceride Lipase from Human Postheparin Plasma by Apolipoproteins A-I and A-II</title><author>KUBO, Masaharu ; 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The experimental data could well be described by a model in which apolipoproteins bound to the surface of lipid substrate particles inhibited the enzyme reaction. The values of Km obtained were similar with or without inhibitors and the calculated saturation levels of apolipoprotein binding to the lipid were in good agreement with those obtained in independent binding experiments.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>6815170</pmid><doi>10.1093/oxfordjournals.jbchem.a134000</doi><tpages>6</tpages></addata></record> |
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source | J-STAGE Free; MEDLINE; Oxford University Press Journals Digital Archive Legacy; Free Full-Text Journals in Chemistry |
subjects | Adult Apolipoprotein A-I Apolipoprotein A-II Apolipoproteins - isolation & purification Apolipoproteins - pharmacology Chemical Phenomena Chemistry Heparin - pharmacology Humans Kinetics Lipase - antagonists & inhibitors Lipase - blood Liver - enzymology Male man plasma triacylglycerol lipase triglycerides |
title | Mechanism of Inhibition of Hepatic Triglyceride Lipase from Human Postheparin Plasma by Apolipoproteins A-I and A-II |
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