Isolation and characterization of proteases from Euphorbia lactea and Euphorbia lactea cristata
Latex from E. lactea yielded three homogeneous proteases, euphorbains, 1a1, 1a2 and 1a3 with Mr of 66 k, 44 k and 33 k respectively. Euphorbains 1a1 and 1a3 had unique pIs of, in order, 7.0 and 4.5, while 1a2 comprised three charged forms with pIs ranging from 5.0 to 6.4. From the latex of E. lactea...
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| Veröffentlicht in: | Phytochemistry (Oxford) 1986, Vol.25 (4), p.807-810 |
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| container_title | Phytochemistry (Oxford) |
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| creator | Lynn, K.R. Clevette-Radford, N.A. |
| description | Latex from E. lactea yielded three homogeneous proteases, euphorbains, 1a1, 1a2 and 1a3 with Mr of 66 k, 44 k and 33 k respectively. Euphorbains 1a1 and 1a3 had unique pIs of, in order, 7.0 and 4.5, while 1a2 comprised three charged forms with pIs ranging from 5.0 to 6.4. From the latex of E. lactea cristata a single proteolytic euphorbain 1c was isolated which had an Mr of 70 000 and five pIs between 5.0 and 8.0. Euphorbains 1a1 and 1c have similar substrate specificities which are different from those of 1a2 and 1a3. Euphorbains 1a1, 1a2 and 1c are serine-centred enzymes with vital histidine residues, and the latter protease is activated by Ca2+, Mg2+ and Mn2+. |
| doi_str_mv | 10.1016/0031-9422(86)80006-1 |
| format | Article |
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Euphorbains 1a1 and 1a3 had unique pIs of, in order, 7.0 and 4.5, while 1a2 comprised three charged forms with pIs ranging from 5.0 to 6.4. From the latex of E. lactea cristata a single proteolytic euphorbain 1c was isolated which had an Mr of 70 000 and five pIs between 5.0 and 8.0. Euphorbains 1a1 and 1c have similar substrate specificities which are different from those of 1a2 and 1a3. Euphorbains 1a1, 1a2 and 1c are serine-centred enzymes with vital histidine residues, and the latter protease is activated by Ca2+, Mg2+ and Mn2+.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><identifier>DOI: 10.1016/0031-9422(86)80006-1</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>amino acid composition ; Analysis of complex biological substances ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; cristata ; enzyme activity ; euphorbain 1a ; euphorbain 1c ; Euphorbia ; Euphorbia lactea ; Euphorbia lactea cristata ; Euphorbiaceae ; Fundamental and applied biological sciences. Psychology ; latex ; Plants and fungi ; proteinase ; proteinases ; purification ; serine protease</subject><ispartof>Phytochemistry (Oxford), 1986, Vol.25 (4), p.807-810</ispartof><rights>1986</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-630b806fa8f859ec325c2b2ec7d69d6e8fe3d7fb11085af4ae860447dbdab5cd3</citedby><cites>FETCH-LOGICAL-c388t-630b806fa8f859ec325c2b2ec7d69d6e8fe3d7fb11085af4ae860447dbdab5cd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0031-9422(86)80006-1$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8637280$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Lynn, K.R.</creatorcontrib><creatorcontrib>Clevette-Radford, N.A.</creatorcontrib><title>Isolation and characterization of proteases from Euphorbia lactea and Euphorbia lactea cristata</title><title>Phytochemistry (Oxford)</title><description>Latex from E. lactea yielded three homogeneous proteases, euphorbains, 1a1, 1a2 and 1a3 with Mr of 66 k, 44 k and 33 k respectively. Euphorbains 1a1 and 1a3 had unique pIs of, in order, 7.0 and 4.5, while 1a2 comprised three charged forms with pIs ranging from 5.0 to 6.4. From the latex of E. lactea cristata a single proteolytic euphorbain 1c was isolated which had an Mr of 70 000 and five pIs between 5.0 and 8.0. Euphorbains 1a1 and 1c have similar substrate specificities which are different from those of 1a2 and 1a3. Euphorbains 1a1, 1a2 and 1c are serine-centred enzymes with vital histidine residues, and the latter protease is activated by Ca2+, Mg2+ and Mn2+.</description><subject>amino acid composition</subject><subject>Analysis of complex biological substances</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>cristata</subject><subject>enzyme activity</subject><subject>euphorbain 1a</subject><subject>euphorbain 1c</subject><subject>Euphorbia</subject><subject>Euphorbia lactea</subject><subject>Euphorbia lactea cristata</subject><subject>Euphorbiaceae</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>latex</subject><subject>Plants and fungi</subject><subject>proteinase</subject><subject>proteinases</subject><subject>purification</subject><subject>serine protease</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><recordid>eNp9kE9L9DAQh4MouK5-A-HtQUQP1UnTptmLIOI_EDyo5zBNJpqXbrMmXUE_va0VL4KngeH5_WZ4GNvncMKBy1MAwfNFWRRHSh4rAJA532AzrmqRixpgk81-kG22k9L_gakqKWdM36bQYu9Dl2FnM_OCEU1P0X9My-CyVQw9YaKUuRiW2eV69RJi4zFrRxK_cr-WJvrUY4-7bMthm2jve87Z09Xl48VNfnd_fXtxfpcboVSfSwGNAulQOVUtyIiiMkVTkKmtXFhJypGwtWs4B1WhK5GUhLKsbWOxqYwVc3Y49Q7fvq4p9Xrpk6G2xY7COmleSgVCygEsJ9DEkFIkp1fRLzG-aw56tKlHVXpUpZXUXzY1H2IH3_2YDLYuYmd8-skqKepiODBn_ybMYdD4PEjQTw8FcAG8rIbzY9HZRNBg481T1Ml46gxZH8n02gb_9yefgaCTTw</recordid><startdate>1986</startdate><enddate>1986</enddate><creator>Lynn, K.R.</creator><creator>Clevette-Radford, N.A.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>1986</creationdate><title>Isolation and characterization of proteases from Euphorbia lactea and Euphorbia lactea cristata</title><author>Lynn, K.R. ; Clevette-Radford, N.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-630b806fa8f859ec325c2b2ec7d69d6e8fe3d7fb11085af4ae860447dbdab5cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>amino acid composition</topic><topic>Analysis of complex biological substances</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>cristata</topic><topic>enzyme activity</topic><topic>euphorbain 1a</topic><topic>euphorbain 1c</topic><topic>Euphorbia</topic><topic>Euphorbia lactea</topic><topic>Euphorbia lactea cristata</topic><topic>Euphorbiaceae</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>latex</topic><topic>Plants and fungi</topic><topic>proteinase</topic><topic>proteinases</topic><topic>purification</topic><topic>serine protease</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lynn, K.R.</creatorcontrib><creatorcontrib>Clevette-Radford, N.A.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lynn, K.R.</au><au>Clevette-Radford, N.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of proteases from Euphorbia lactea and Euphorbia lactea cristata</atitle><jtitle>Phytochemistry (Oxford)</jtitle><date>1986</date><risdate>1986</risdate><volume>25</volume><issue>4</issue><spage>807</spage><epage>810</epage><pages>807-810</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>Latex from E. lactea yielded three homogeneous proteases, euphorbains, 1a1, 1a2 and 1a3 with Mr of 66 k, 44 k and 33 k respectively. Euphorbains 1a1 and 1a3 had unique pIs of, in order, 7.0 and 4.5, while 1a2 comprised three charged forms with pIs ranging from 5.0 to 6.4. From the latex of E. lactea cristata a single proteolytic euphorbain 1c was isolated which had an Mr of 70 000 and five pIs between 5.0 and 8.0. Euphorbains 1a1 and 1c have similar substrate specificities which are different from those of 1a2 and 1a3. Euphorbains 1a1, 1a2 and 1c are serine-centred enzymes with vital histidine residues, and the latter protease is activated by Ca2+, Mg2+ and Mn2+.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><doi>10.1016/0031-9422(86)80006-1</doi><tpages>4</tpages></addata></record> |
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| ispartof | Phytochemistry (Oxford), 1986, Vol.25 (4), p.807-810 |
| issn | 0031-9422 1873-3700 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete |
| subjects | amino acid composition Analysis of complex biological substances Analytical, structural and metabolic biochemistry Biological and medical sciences cristata enzyme activity euphorbain 1a euphorbain 1c Euphorbia Euphorbia lactea Euphorbia lactea cristata Euphorbiaceae Fundamental and applied biological sciences. Psychology latex Plants and fungi proteinase proteinases purification serine protease |
| title | Isolation and characterization of proteases from Euphorbia lactea and Euphorbia lactea cristata |
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