Structure and Properties of a Human Non-pancreatic Phospholipase A2
We have purified a human non-pancreatic phospholipase A2 that is present in platelets and is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH optimum of 8–10, and shows a striking preference for substrate presented in the form of Escherichia coli membranes. In the E....
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| Veröffentlicht in: | The Journal of biological chemistry 1989-04, Vol.264 (10), p.5768-5775 |
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| container_issue | 10 |
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| container_title | The Journal of biological chemistry |
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| creator | Kramer, R M Hession, C Johansen, B Hayes, G McGray, P Chow, E P Tizard, R Pepinsky, R B |
| description | We have purified a human non-pancreatic phospholipase A2 that is present in platelets and is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH optimum of 8–10, and shows a striking preference for substrate presented in the form of Escherichia coli membranes. In the E. coli phospholipase A2 assay the phospholipase exhibits an apparent specific activity of 300 µmol/mg/min. Using oligonucleotide probes based on amino-terminal sequence data, we cloned the corresponding human gene from a genomic DNA library and expressed the gene in animal cells. The protein was secreted from the cells in an active form. The deduced amino acid sequence of the human protein consists of 124 amino acids, contains structural features common to all known phospholipase A2s, and has a half-cystine pattern that is characteristic of the snake venom group II enzymes. |
| doi_str_mv | 10.1016/S0021-9258(18)83616-X |
| format | Article |
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The enzyme is calcium-dependent, has a pH optimum of 8–10, and shows a striking preference for substrate presented in the form of Escherichia coli membranes. In the E. coli phospholipase A2 assay the phospholipase exhibits an apparent specific activity of 300 µmol/mg/min. Using oligonucleotide probes based on amino-terminal sequence data, we cloned the corresponding human gene from a genomic DNA library and expressed the gene in animal cells. The protein was secreted from the cells in an active form. 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Technologies ; Molecular and cellular biology ; Molecular cloning ; Molecular genetics ; Molecular Sequence Data ; Molecular Weight ; Organ Specificity ; Pancreas - enzymology ; Phospholipases - genetics ; Phospholipases A - genetics ; Phospholipases A - isolation & purification ; Phospholipases A - metabolism ; Phospholipases A2 ; Restriction Mapping ; Synovial Fluid - enzymology</subject><ispartof>The Journal of biological chemistry, 1989-04, Vol.264 (10), p.5768-5775</ispartof><rights>1989 © 1989 ASBMB. 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The enzyme is calcium-dependent, has a pH optimum of 8–10, and shows a striking preference for substrate presented in the form of Escherichia coli membranes. In the E. coli phospholipase A2 assay the phospholipase exhibits an apparent specific activity of 300 µmol/mg/min. Using oligonucleotide probes based on amino-terminal sequence data, we cloned the corresponding human gene from a genomic DNA library and expressed the gene in animal cells. The protein was secreted from the cells in an active form. The deduced amino acid sequence of the human protein consists of 124 amino acids, contains structural features common to all known phospholipase A2s, and has a half-cystine pattern that is characteristic of the snake venom group II enzymes.</description><subject>Amino Acid Sequence</subject><subject>Arthritis, Rheumatoid - enzymology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Blood Platelets - enzymology</subject><subject>Chromatography, Gel</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genes. Genome</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular and cellular biology</subject><subject>Molecular cloning</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Organ Specificity</subject><subject>Pancreas - enzymology</subject><subject>Phospholipases - genetics</subject><subject>Phospholipases A - genetics</subject><subject>Phospholipases A - isolation & purification</subject><subject>Phospholipases A - metabolism</subject><subject>Phospholipases A2</subject><subject>Restriction Mapping</subject><subject>Synovial Fluid - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3DAQhkVpSTZpf0LA0BKSg1t9WvIphCVtCqENpIW9CVkexSq25Uh2Sv99tdllr9FlQPO8M8OD0BnBnwkm1ZcHjCkpayrUBVGXilWkKjdv0IpgxUomyOYtWh2QY3SS0h-cH6_JETqi-bNibIXWD3Nc7LxEKMzYFvcxTBBnD6kIrjDF7TKYsfgRxnIyo41gZm-L-y6kqQu9n0yC4pq-R--c6RN82NdT9Pvrza_1bXn389v39fVdaQXDc0kNd5LLhignjLPgRANCOCJUw5W0FJSTDJtatc7xuq5qqlgtuKXSEiMoZ6fofDd3iuFpgTTrwScLfW9GCEvSUqm6EhJnUOxAG0NKEZyeoh9M_KcJ1lt5-kWe3prRROkXeXqTc2f7BUszQHtI7W3l_qd93yRrehezE58OmGSEML7FPu6wzj92f30E3fhgOxg0rfj2BCErlamrHQVZ2bOHqJP1MFpoc8LOug3-lXP_A4hElh0</recordid><startdate>19890405</startdate><enddate>19890405</enddate><creator>Kramer, R M</creator><creator>Hession, C</creator><creator>Johansen, B</creator><creator>Hayes, G</creator><creator>McGray, P</creator><creator>Chow, E P</creator><creator>Tizard, R</creator><creator>Pepinsky, R B</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19890405</creationdate><title>Structure and Properties of a Human Non-pancreatic Phospholipase A2</title><author>Kramer, R M ; Hession, C ; Johansen, B ; Hayes, G ; McGray, P ; Chow, E P ; Tizard, R ; Pepinsky, R B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-2a4f747b18f5afcef5be55f158b487c2e8f730a98dff49969283954c27c1a5243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Arthritis, Rheumatoid - enzymology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Blood Platelets - enzymology</topic><topic>Chromatography, Gel</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Genes. Genome</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular and cellular biology</topic><topic>Molecular cloning</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Organ Specificity</topic><topic>Pancreas - enzymology</topic><topic>Phospholipases - genetics</topic><topic>Phospholipases A - genetics</topic><topic>Phospholipases A - isolation & purification</topic><topic>Phospholipases A - metabolism</topic><topic>Phospholipases A2</topic><topic>Restriction Mapping</topic><topic>Synovial Fluid - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kramer, R M</creatorcontrib><creatorcontrib>Hession, C</creatorcontrib><creatorcontrib>Johansen, B</creatorcontrib><creatorcontrib>Hayes, G</creatorcontrib><creatorcontrib>McGray, P</creatorcontrib><creatorcontrib>Chow, E P</creatorcontrib><creatorcontrib>Tizard, R</creatorcontrib><creatorcontrib>Pepinsky, R B</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kramer, R M</au><au>Hession, C</au><au>Johansen, B</au><au>Hayes, G</au><au>McGray, P</au><au>Chow, E P</au><au>Tizard, R</au><au>Pepinsky, R B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and Properties of a Human Non-pancreatic Phospholipase A2</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-04-05</date><risdate>1989</risdate><volume>264</volume><issue>10</issue><spage>5768</spage><epage>5775</epage><pages>5768-5775</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have purified a human non-pancreatic phospholipase A2 that is present in platelets and is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH optimum of 8–10, and shows a striking preference for substrate presented in the form of Escherichia coli membranes. In the E. coli phospholipase A2 assay the phospholipase exhibits an apparent specific activity of 300 µmol/mg/min. Using oligonucleotide probes based on amino-terminal sequence data, we cloned the corresponding human gene from a genomic DNA library and expressed the gene in animal cells. The protein was secreted from the cells in an active form. The deduced amino acid sequence of the human protein consists of 124 amino acids, contains structural features common to all known phospholipase A2s, and has a half-cystine pattern that is characteristic of the snake venom group II enzymes.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2925633</pmid><doi>10.1016/S0021-9258(18)83616-X</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Arthritis, Rheumatoid - enzymology Base Sequence Biological and medical sciences Biotechnology Blood Platelets - enzymology Chromatography, Gel Chromatography, High Pressure Liquid Chromatography, Ion Exchange Fundamental and applied biological sciences. Psychology Genes Genes. Genome Genetic engineering Genetic technics Humans Kinetics Methods. Procedures. Technologies Molecular and cellular biology Molecular cloning Molecular genetics Molecular Sequence Data Molecular Weight Organ Specificity Pancreas - enzymology Phospholipases - genetics Phospholipases A - genetics Phospholipases A - isolation & purification Phospholipases A - metabolism Phospholipases A2 Restriction Mapping Synovial Fluid - enzymology |
| title | Structure and Properties of a Human Non-pancreatic Phospholipase A2 |
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