Secretion of an active recombinant dog gastric lipase from baculovirus-infected insect cells

An active dog gastric lipase (DGL) belonging to the acid-stable mammalian lipase family, was produced and secreted from baculovirus-infected insect cells using the honeybee melittin and the DGL signal sequences. Both sequences drove the secretion of an active 47 kDa recombinant DGL (rDGL). rDGL was...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biotechnology letters 1998-07, Vol.20 (7), p.697-702
Hauptverfasser: JOLIFF, G, VAGANAY, S, LEGAY, C, BENICOURT, C
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 702
container_issue 7
container_start_page 697
container_title Biotechnology letters
container_volume 20
creator JOLIFF, G
VAGANAY, S
LEGAY, C
BENICOURT, C
description An active dog gastric lipase (DGL) belonging to the acid-stable mammalian lipase family, was produced and secreted from baculovirus-infected insect cells using the honeybee melittin and the DGL signal sequences. Both sequences drove the secretion of an active 47 kDa recombinant DGL (rDGL). rDGL was secreted at about 35 mg/L of culture medium. A one step purification using a cation exchange chromatography was used to recover an active electrophoretically pure rDGL from 2 days post-infection supernatant. There were not significant differences between the enzymatic properties of native and recombinant proteins. © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]
doi_str_mv 10.1023/A:1005330826017
format Article
fullrecord <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_proquest_miscellaneous_16554783</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16554783</sourcerecordid><originalsourceid>FETCH-LOGICAL-p240t-28efd6c9c517af840532b0dc3a6a2b0572697738c48b1b37b6f9ad260a3bbdd23</originalsourceid><addsrcrecordid>eNpdj0tLxDAUhYMoOI6u3QYRd9W8mrTuhsEXDLhQd0K5SZMhQ5vUpB3w31txVq7OWXycB0KXlNxSwvjd6p4SUnJOKiYJVUdoQUvFC6mUPEYLQgUtSlGzU3SW844QUiuiFujzzZpkRx8Djg5DwGBGv7c4WRN77QOEEbdxi7eQx-QN7vwA2WKXYo81mKmLe5-mXPjgrBlti33Is8HGdl0-RycOumwvDrpEH48P7-vnYvP69LJebYqBCTIWrLKulaY2JVXgKjG_YJq0hoOE2ZSKyVopXhlRaaq50tLV0M4vgWvdtowv0c1f7pDi12Tz2PQ-_y6AYOOUGyrLUqiKz-DVP3AXpxTmbY3ioiZzt5ih6wME2UDnEgTjczMk30P6bphgRErCfwDUVG-G</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>734908404</pqid></control><display><type>article</type><title>Secretion of an active recombinant dog gastric lipase from baculovirus-infected insect cells</title><source>SpringerLink Journals</source><creator>JOLIFF, G ; VAGANAY, S ; LEGAY, C ; BENICOURT, C</creator><creatorcontrib>JOLIFF, G ; VAGANAY, S ; LEGAY, C ; BENICOURT, C</creatorcontrib><description>An active dog gastric lipase (DGL) belonging to the acid-stable mammalian lipase family, was produced and secreted from baculovirus-infected insect cells using the honeybee melittin and the DGL signal sequences. Both sequences drove the secretion of an active 47 kDa recombinant DGL (rDGL). rDGL was secreted at about 35 mg/L of culture medium. A one step purification using a cation exchange chromatography was used to recover an active electrophoretically pure rDGL from 2 days post-infection supernatant. There were not significant differences between the enzymatic properties of native and recombinant proteins. © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1023/A:1005330826017</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Apis mellifera ; Biological and medical sciences ; Biotechnology ; Cation exchange ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Genetic technics ; Insecta ; Insects ; Methods. Procedures. Technologies ; Modification of gene expression level ; Proteins</subject><ispartof>Biotechnology letters, 1998-07, Vol.20 (7), p.697-702</ispartof><rights>1998 INIST-CNRS</rights><rights>Chapman and Hall 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=2420660$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>JOLIFF, G</creatorcontrib><creatorcontrib>VAGANAY, S</creatorcontrib><creatorcontrib>LEGAY, C</creatorcontrib><creatorcontrib>BENICOURT, C</creatorcontrib><title>Secretion of an active recombinant dog gastric lipase from baculovirus-infected insect cells</title><title>Biotechnology letters</title><description>An active dog gastric lipase (DGL) belonging to the acid-stable mammalian lipase family, was produced and secreted from baculovirus-infected insect cells using the honeybee melittin and the DGL signal sequences. Both sequences drove the secretion of an active 47 kDa recombinant DGL (rDGL). rDGL was secreted at about 35 mg/L of culture medium. A one step purification using a cation exchange chromatography was used to recover an active electrophoretically pure rDGL from 2 days post-infection supernatant. There were not significant differences between the enzymatic properties of native and recombinant proteins. © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]</description><subject>Apis mellifera</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cation exchange</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Insecta</subject><subject>Insects</subject><subject>Methods. Procedures. Technologies</subject><subject>Modification of gene expression level</subject><subject>Proteins</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdj0tLxDAUhYMoOI6u3QYRd9W8mrTuhsEXDLhQd0K5SZMhQ5vUpB3w31txVq7OWXycB0KXlNxSwvjd6p4SUnJOKiYJVUdoQUvFC6mUPEYLQgUtSlGzU3SW844QUiuiFujzzZpkRx8Djg5DwGBGv7c4WRN77QOEEbdxi7eQx-QN7vwA2WKXYo81mKmLe5-mXPjgrBlti33Is8HGdl0-RycOumwvDrpEH48P7-vnYvP69LJebYqBCTIWrLKulaY2JVXgKjG_YJq0hoOE2ZSKyVopXhlRaaq50tLV0M4vgWvdtowv0c1f7pDi12Tz2PQ-_y6AYOOUGyrLUqiKz-DVP3AXpxTmbY3ioiZzt5ih6wME2UDnEgTjczMk30P6bphgRErCfwDUVG-G</recordid><startdate>19980701</startdate><enddate>19980701</enddate><creator>JOLIFF, G</creator><creator>VAGANAY, S</creator><creator>LEGAY, C</creator><creator>BENICOURT, C</creator><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7QO</scope><scope>7SS</scope></search><sort><creationdate>19980701</creationdate><title>Secretion of an active recombinant dog gastric lipase from baculovirus-infected insect cells</title><author>JOLIFF, G ; VAGANAY, S ; LEGAY, C ; BENICOURT, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p240t-28efd6c9c517af840532b0dc3a6a2b0572697738c48b1b37b6f9ad260a3bbdd23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Apis mellifera</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cation exchange</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Insecta</topic><topic>Insects</topic><topic>Methods. Procedures. Technologies</topic><topic>Modification of gene expression level</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>JOLIFF, G</creatorcontrib><creatorcontrib>VAGANAY, S</creatorcontrib><creatorcontrib>LEGAY, C</creatorcontrib><creatorcontrib>BENICOURT, C</creatorcontrib><collection>Pascal-Francis</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</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>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</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>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>JOLIFF, G</au><au>VAGANAY, S</au><au>LEGAY, C</au><au>BENICOURT, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Secretion of an active recombinant dog gastric lipase from baculovirus-infected insect cells</atitle><jtitle>Biotechnology letters</jtitle><date>1998-07-01</date><risdate>1998</risdate><volume>20</volume><issue>7</issue><spage>697</spage><epage>702</epage><pages>697-702</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>An active dog gastric lipase (DGL) belonging to the acid-stable mammalian lipase family, was produced and secreted from baculovirus-infected insect cells using the honeybee melittin and the DGL signal sequences. Both sequences drove the secretion of an active 47 kDa recombinant DGL (rDGL). rDGL was secreted at about 35 mg/L of culture medium. A one step purification using a cation exchange chromatography was used to recover an active electrophoretically pure rDGL from 2 days post-infection supernatant. There were not significant differences between the enzymatic properties of native and recombinant proteins. © Rapid Science Ltd. 1998[PUBLICATION ABSTRACT]</abstract><cop>Dordrecht</cop><pub>Springer</pub><doi>10.1023/A:1005330826017</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0141-5492
ispartof Biotechnology letters, 1998-07, Vol.20 (7), p.697-702
issn 0141-5492
1573-6776
language eng
recordid cdi_proquest_miscellaneous_16554783
source SpringerLink Journals
subjects Apis mellifera
Biological and medical sciences
Biotechnology
Cation exchange
Enzymes
Fundamental and applied biological sciences. Psychology
Genetic engineering
Genetic technics
Insecta
Insects
Methods. Procedures. Technologies
Modification of gene expression level
Proteins
title Secretion of an active recombinant dog gastric lipase from baculovirus-infected insect cells
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T14%3A13%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Secretion%20of%20an%20active%20recombinant%20dog%20gastric%20lipase%20from%20baculovirus-infected%20insect%20cells&rft.jtitle=Biotechnology%20letters&rft.au=JOLIFF,%20G&rft.date=1998-07-01&rft.volume=20&rft.issue=7&rft.spage=697&rft.epage=702&rft.pages=697-702&rft.issn=0141-5492&rft.eissn=1573-6776&rft.coden=BILED3&rft_id=info:doi/10.1023/A:1005330826017&rft_dat=%3Cproquest_pasca%3E16554783%3C/proquest_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=734908404&rft_id=info:pmid/&rfr_iscdi=true