Analysis of Leishmania proteinases reveals developmental changes in species‐specific forms and a common 68‐kDa activity
The proteinases of three species of Leishmania have been analysed by electrophoresis. Amastigotes of L. mexicana mexicana have several high‐activity, low‐Mr cysteine proteinases which are absent from log‐phase promastigotes of L. m. mexicana and from all developmental stages of the other species ana...
Gespeichert in:
| Veröffentlicht in: | FEMS microbiology letters 1987-12, Vol.48 (3), p.345-350 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 350 |
|---|---|
| container_issue | 3 |
| container_start_page | 345 |
| container_title | FEMS microbiology letters |
| container_volume | 48 |
| creator | Lockwood, Barbara C. North, Michael J. Mallinson, David J. Coombs, Graham H. |
| description | The proteinases of three species of Leishmania have been analysed by electrophoresis. Amastigotes of L. mexicana mexicana have several high‐activity, low‐Mr cysteine proteinases which are absent from log‐phase promastigotes of L. m. mexicana and from all developmental stages of the other species analysed (L. donovani and L. major). Low‐activity, low‐Mr proteinases were present in populations of stationary‐phase promastigotes of L. m. mexicana. All three species of Leishmania had higher Mr proteinases, a number of which showed developmental regulation, some of them being stage‐specific. Significantly, at all stages of the life cycle in all three species a 68‐kDa proteinase was apparent. In its size, sensitivity to inhibitors and ability to bind concanavalin A‐agarose, this resembles the major surface protein thought to be present in all Leishmania species and which has recently been reported to possess proteinase activity in L. major promastigotes. |
| doi_str_mv | 10.1111/j.1574-6968.1987.tb02622.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_14848432</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>14848432</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2915-7f6de25ca9f9ccc47c9ad93e463ce13953da8c2380a337818ac46844ab077b893</originalsourceid><addsrcrecordid>eNqVkMFu1DAQhi1EpS5t38FCiFuCHTuxzQGpaikgLeqFnq3ZiUO9JM6SSUtXXPoIPCNPUi-76h37MJbm8z-aj7HXUpQyn3frUtZGF41rbCmdNeW8ElVTVeXDC7Z4br1kC6GMLaRw5pi9IloLIXQlmgX7fZ6g31IkPnZ8GSLdDpAi8M00ziEmoEB8CvcBeuJtrv24GUKaoed4C-l77sbEaRMwBvr7-Offq4vIu3EaiENqOXAch2FMvLEZ-HEJHHCO93HenrKjLueGs0M9YTdXH79dfC6W15--XJwvC6ycrAvTNW2oagTXOUTUBh20TgXdKAxSuVq1YLFSVoDKW0oLqBurNayEMSvr1Al7u8_NS_28CzT7IRKGvocUxjvyUtt8VZXB93sQp5FoCp3fTHGAaeul8Dvffu13Uv1Oqt_59gff_iF_fnOYAoTQdxMkjPScYIyWtbIZ-7DHfsU-bP9jgL_6ulS6Vk95sZkI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14848432</pqid></control><display><type>article</type><title>Analysis of Leishmania proteinases reveals developmental changes in species‐specific forms and a common 68‐kDa activity</title><source>Oxford University Press Journals Digital Archive legacy</source><source>Access via Wiley Online Library</source><source>Alma/SFX Local Collection</source><creator>Lockwood, Barbara C. ; North, Michael J. ; Mallinson, David J. ; Coombs, Graham H.</creator><creatorcontrib>Lockwood, Barbara C. ; North, Michael J. ; Mallinson, David J. ; Coombs, Graham H.</creatorcontrib><description>The proteinases of three species of Leishmania have been analysed by electrophoresis. Amastigotes of L. mexicana mexicana have several high‐activity, low‐Mr cysteine proteinases which are absent from log‐phase promastigotes of L. m. mexicana and from all developmental stages of the other species analysed (L. donovani and L. major). Low‐activity, low‐Mr proteinases were present in populations of stationary‐phase promastigotes of L. m. mexicana. All three species of Leishmania had higher Mr proteinases, a number of which showed developmental regulation, some of them being stage‐specific. Significantly, at all stages of the life cycle in all three species a 68‐kDa proteinase was apparent. In its size, sensitivity to inhibitors and ability to bind concanavalin A‐agarose, this resembles the major surface protein thought to be present in all Leishmania species and which has recently been reported to possess proteinase activity in L. major promastigotes.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1987.tb02622.x</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Development ; electrophoresis ; Fundamental and applied biological sciences. Psychology ; L. donovani ; L. major ; Leishmania ; Leishmania donovani ; Leishmania major ; Leishmania mexicana ; Leishmania mexicana mexicana ; proteinase ; Proteinases ; Protozoa</subject><ispartof>FEMS microbiology letters, 1987-12, Vol.48 (3), p.345-350</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2915-7f6de25ca9f9ccc47c9ad93e463ce13953da8c2380a337818ac46844ab077b893</citedby><cites>FETCH-LOGICAL-c2915-7f6de25ca9f9ccc47c9ad93e463ce13953da8c2380a337818ac46844ab077b893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1987.tb02622.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1987.tb02622.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7741538$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Lockwood, Barbara C.</creatorcontrib><creatorcontrib>North, Michael J.</creatorcontrib><creatorcontrib>Mallinson, David J.</creatorcontrib><creatorcontrib>Coombs, Graham H.</creatorcontrib><title>Analysis of Leishmania proteinases reveals developmental changes in species‐specific forms and a common 68‐kDa activity</title><title>FEMS microbiology letters</title><description>The proteinases of three species of Leishmania have been analysed by electrophoresis. Amastigotes of L. mexicana mexicana have several high‐activity, low‐Mr cysteine proteinases which are absent from log‐phase promastigotes of L. m. mexicana and from all developmental stages of the other species analysed (L. donovani and L. major). Low‐activity, low‐Mr proteinases were present in populations of stationary‐phase promastigotes of L. m. mexicana. All three species of Leishmania had higher Mr proteinases, a number of which showed developmental regulation, some of them being stage‐specific. Significantly, at all stages of the life cycle in all three species a 68‐kDa proteinase was apparent. In its size, sensitivity to inhibitors and ability to bind concanavalin A‐agarose, this resembles the major surface protein thought to be present in all Leishmania species and which has recently been reported to possess proteinase activity in L. major promastigotes.</description><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Development</subject><subject>electrophoresis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>L. donovani</subject><subject>L. major</subject><subject>Leishmania</subject><subject>Leishmania donovani</subject><subject>Leishmania major</subject><subject>Leishmania mexicana</subject><subject>Leishmania mexicana mexicana</subject><subject>proteinase</subject><subject>Proteinases</subject><subject>Protozoa</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNqVkMFu1DAQhi1EpS5t38FCiFuCHTuxzQGpaikgLeqFnq3ZiUO9JM6SSUtXXPoIPCNPUi-76h37MJbm8z-aj7HXUpQyn3frUtZGF41rbCmdNeW8ElVTVeXDC7Z4br1kC6GMLaRw5pi9IloLIXQlmgX7fZ6g31IkPnZ8GSLdDpAi8M00ziEmoEB8CvcBeuJtrv24GUKaoed4C-l77sbEaRMwBvr7-Offq4vIu3EaiENqOXAch2FMvLEZ-HEJHHCO93HenrKjLueGs0M9YTdXH79dfC6W15--XJwvC6ycrAvTNW2oagTXOUTUBh20TgXdKAxSuVq1YLFSVoDKW0oLqBurNayEMSvr1Al7u8_NS_28CzT7IRKGvocUxjvyUtt8VZXB93sQp5FoCp3fTHGAaeul8Dvffu13Uv1Oqt_59gff_iF_fnOYAoTQdxMkjPScYIyWtbIZ-7DHfsU-bP9jgL_6ulS6Vk95sZkI</recordid><startdate>198712</startdate><enddate>198712</enddate><creator>Lockwood, Barbara C.</creator><creator>North, Michael J.</creator><creator>Mallinson, David J.</creator><creator>Coombs, Graham H.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>M7N</scope></search><sort><creationdate>198712</creationdate><title>Analysis of Leishmania proteinases reveals developmental changes in species‐specific forms and a common 68‐kDa activity</title><author>Lockwood, Barbara C. ; North, Michael J. ; Mallinson, David J. ; Coombs, Graham H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2915-7f6de25ca9f9ccc47c9ad93e463ce13953da8c2380a337818ac46844ab077b893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Development</topic><topic>electrophoresis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>L. donovani</topic><topic>L. major</topic><topic>Leishmania</topic><topic>Leishmania donovani</topic><topic>Leishmania major</topic><topic>Leishmania mexicana</topic><topic>Leishmania mexicana mexicana</topic><topic>proteinase</topic><topic>Proteinases</topic><topic>Protozoa</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lockwood, Barbara C.</creatorcontrib><creatorcontrib>North, Michael J.</creatorcontrib><creatorcontrib>Mallinson, David J.</creatorcontrib><creatorcontrib>Coombs, Graham H.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lockwood, Barbara C.</au><au>North, Michael J.</au><au>Mallinson, David J.</au><au>Coombs, Graham H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of Leishmania proteinases reveals developmental changes in species‐specific forms and a common 68‐kDa activity</atitle><jtitle>FEMS microbiology letters</jtitle><date>1987-12</date><risdate>1987</risdate><volume>48</volume><issue>3</issue><spage>345</spage><epage>350</epage><pages>345-350</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>The proteinases of three species of Leishmania have been analysed by electrophoresis. Amastigotes of L. mexicana mexicana have several high‐activity, low‐Mr cysteine proteinases which are absent from log‐phase promastigotes of L. m. mexicana and from all developmental stages of the other species analysed (L. donovani and L. major). Low‐activity, low‐Mr proteinases were present in populations of stationary‐phase promastigotes of L. m. mexicana. All three species of Leishmania had higher Mr proteinases, a number of which showed developmental regulation, some of them being stage‐specific. Significantly, at all stages of the life cycle in all three species a 68‐kDa proteinase was apparent. In its size, sensitivity to inhibitors and ability to bind concanavalin A‐agarose, this resembles the major surface protein thought to be present in all Leishmania species and which has recently been reported to possess proteinase activity in L. major promastigotes.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1574-6968.1987.tb02622.x</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1987-12, Vol.48 (3), p.345-350 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_14848432 |
| source | Oxford University Press Journals Digital Archive legacy; Access via Wiley Online Library; Alma/SFX Local Collection |
| subjects | Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Development electrophoresis Fundamental and applied biological sciences. Psychology L. donovani L. major Leishmania Leishmania donovani Leishmania major Leishmania mexicana Leishmania mexicana mexicana proteinase Proteinases Protozoa |
| title | Analysis of Leishmania proteinases reveals developmental changes in species‐specific forms and a common 68‐kDa activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T01%3A55%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Analysis%20of%20Leishmania%20proteinases%20reveals%20developmental%20changes%20in%20species%E2%80%90specific%20forms%20and%20a%20common%2068%E2%80%90kDa%20activity&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Lockwood,%20Barbara%20C.&rft.date=1987-12&rft.volume=48&rft.issue=3&rft.spage=345&rft.epage=350&rft.pages=345-350&rft.issn=0378-1097&rft.eissn=1574-6968&rft.coden=FMLED7&rft_id=info:doi/10.1111/j.1574-6968.1987.tb02622.x&rft_dat=%3Cproquest_cross%3E14848432%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14848432&rft_id=info:pmid/&rfr_iscdi=true |