Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase
A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate...
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| Veröffentlicht in: | Parasitology 2016-04, Vol.143 (5), p.646-657 |
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| creator | IGETEI, JOSEPH E. LIDDELL, SUSAN EL-FAHAM, MARWA DOENHOFF, MICHAEL J. |
| description | A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion. |
| doi_str_mv | 10.1017/S0031182016000184 |
| format | Article |
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The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion.</description><identifier>ISSN: 0031-1820</identifier><identifier>EISSN: 1469-8161</identifier><identifier>DOI: 10.1017/S0031182016000184</identifier><identifier>PMID: 26924446</identifier><language>eng</language><publisher>Cambridge, UK: Cambridge University Press</publisher><subject>Animals ; Biomphalaria ; Carboxylesterase - blood ; Carboxylesterase - chemistry ; Carboxylesterase - isolation & purification ; Carboxylesterase - metabolism ; Electrophoresis, Polyacrylamide Gel ; Ethanol ; Hydrolysis ; Immunodiffusion ; Immunoprecipitation ; Mass spectrometry ; Mice ; Molecular Weight ; Parasites ; Peptides ; Phenylalanine - analogs & derivatives ; Phenylalanine - metabolism ; Rabbits ; Rats ; Schistosoma mansoni - enzymology ; Serum Albumin - metabolism ; Sodium chloride ; Tandem Mass Spectrometry</subject><ispartof>Parasitology, 2016-04, Vol.143 (5), p.646-657</ispartof><rights>Copyright © Cambridge University Press 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-8e592e0e602eaa3b8c904f8e4aff361ecf8aa36d52a10fc7bc39c29d587cdc723</citedby><cites>FETCH-LOGICAL-c373t-8e592e0e602eaa3b8c904f8e4aff361ecf8aa36d52a10fc7bc39c29d587cdc723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.cambridge.org/core/product/identifier/S0031182016000184/type/journal_article$$EHTML$$P50$$Gcambridge$$H</linktohtml><link.rule.ids>164,314,780,784,27924,27925,55628</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26924446$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>IGETEI, JOSEPH E.</creatorcontrib><creatorcontrib>LIDDELL, SUSAN</creatorcontrib><creatorcontrib>EL-FAHAM, MARWA</creatorcontrib><creatorcontrib>DOENHOFF, MICHAEL J.</creatorcontrib><title>Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase</title><title>Parasitology</title><addtitle>Parasitology</addtitle><description>A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion.</description><subject>Animals</subject><subject>Biomphalaria</subject><subject>Carboxylesterase - blood</subject><subject>Carboxylesterase - chemistry</subject><subject>Carboxylesterase - isolation & purification</subject><subject>Carboxylesterase - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Ethanol</subject><subject>Hydrolysis</subject><subject>Immunodiffusion</subject><subject>Immunoprecipitation</subject><subject>Mass spectrometry</subject><subject>Mice</subject><subject>Molecular Weight</subject><subject>Parasites</subject><subject>Peptides</subject><subject>Phenylalanine - analogs & derivatives</subject><subject>Phenylalanine - metabolism</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Schistosoma mansoni - enzymology</subject><subject>Serum Albumin - metabolism</subject><subject>Sodium chloride</subject><subject>Tandem Mass Spectrometry</subject><issn>0031-1820</issn><issn>1469-8161</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNp1kU-LFDEQxYMo7rj6AbxIwIuX1vzpSaePsqgrLCisnpvqdMXJ2knGJI32fhY_7GaYUUTxVFDvV-8VPEKecvaSM969umZMcq4F44oxxnV7j2x4q_pGc8Xvk81Bbg76GXmU801llFTiITkTqhdt26oN-flxSc46A8XFQKOlQM1u9bGkdZ9daGb3FSmG29Uj3SfMGAqtIEzLXOi12blcYo4eqIeQY3D0e0w-U5uipy5YNAUn6p1BCmGiruRqDwnqOrnbYyjkGrqLuVADaYw_1hlzlSHjY_LAwpzxyWmek89v33y6uGyuPrx7f_H6qjGyk6XRuO0FMlRMIIActelZazW2YK1UHI3Vda2mrQDOrOlGI3sj-mmrOzOZTshz8uLou0_x21LTB--ywXmGgHHJA-86xXTPOlbR53-hN3FJoX43cL1VvWacHSh-pEyKOSe0wz45D2kdOBsO1Q3_VFdvnp2cl9Hj9PviV1cVkCdT8GNy0xf8I_u_tnfJBqbq</recordid><startdate>201604</startdate><enddate>201604</enddate><creator>IGETEI, JOSEPH E.</creator><creator>LIDDELL, SUSAN</creator><creator>EL-FAHAM, MARWA</creator><creator>DOENHOFF, MICHAEL J.</creator><general>Cambridge University Press</general><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>3V.</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201604</creationdate><title>Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase</title><author>IGETEI, JOSEPH E. ; LIDDELL, SUSAN ; EL-FAHAM, MARWA ; DOENHOFF, MICHAEL J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-8e592e0e602eaa3b8c904f8e4aff361ecf8aa36d52a10fc7bc39c29d587cdc723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Biomphalaria</topic><topic>Carboxylesterase - blood</topic><topic>Carboxylesterase - chemistry</topic><topic>Carboxylesterase - isolation & purification</topic><topic>Carboxylesterase - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Ethanol</topic><topic>Hydrolysis</topic><topic>Immunodiffusion</topic><topic>Immunoprecipitation</topic><topic>Mass spectrometry</topic><topic>Mice</topic><topic>Molecular Weight</topic><topic>Parasites</topic><topic>Peptides</topic><topic>Phenylalanine - analogs & derivatives</topic><topic>Phenylalanine - metabolism</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Schistosoma mansoni - enzymology</topic><topic>Serum Albumin - metabolism</topic><topic>Sodium chloride</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>IGETEI, JOSEPH E.</creatorcontrib><creatorcontrib>LIDDELL, SUSAN</creatorcontrib><creatorcontrib>EL-FAHAM, MARWA</creatorcontrib><creatorcontrib>DOENHOFF, MICHAEL J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>IGETEI, JOSEPH E.</au><au>LIDDELL, SUSAN</au><au>EL-FAHAM, MARWA</au><au>DOENHOFF, MICHAEL J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase</atitle><jtitle>Parasitology</jtitle><addtitle>Parasitology</addtitle><date>2016-04</date><risdate>2016</risdate><volume>143</volume><issue>5</issue><spage>646</spage><epage>657</epage><pages>646-657</pages><issn>0031-1820</issn><eissn>1469-8161</eissn><abstract>A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion.</abstract><cop>Cambridge, UK</cop><pub>Cambridge University Press</pub><pmid>26924446</pmid><doi>10.1017/S0031182016000184</doi><tpages>12</tpages></addata></record> |
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| ispartof | Parasitology, 2016-04, Vol.143 (5), p.646-657 |
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| subjects | Animals Biomphalaria Carboxylesterase - blood Carboxylesterase - chemistry Carboxylesterase - isolation & purification Carboxylesterase - metabolism Electrophoresis, Polyacrylamide Gel Ethanol Hydrolysis Immunodiffusion Immunoprecipitation Mass spectrometry Mice Molecular Weight Parasites Peptides Phenylalanine - analogs & derivatives Phenylalanine - metabolism Rabbits Rats Schistosoma mansoni - enzymology Serum Albumin - metabolism Sodium chloride Tandem Mass Spectrometry |
| title | Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase |
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