Taraxalisin – a serine proteinase from dandelion Taraxacum officinale Webb s.l
Latex of dandelion roots contains a serine proteinase that hydrolyzes a chromogenic peptide substrate Glp-Ala-Ala-Leu-pNA optimally at pH 8.0. Maximal activity of the proteinase in the roots is attained in April, at the beginning of plant development after the winter period. The protease was isolate...
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| Veröffentlicht in: | FEBS letters 1998-10, Vol.437 (3), p.237-240 |
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| creator | Rudenskaya, G.N. Bogacheva, A.M. Preusser, A. Kuznetsova, A.V. Dunaevsky, Ya.E. Golovkin, B.N. Stepanov, V.M. |
| description | Latex of dandelion roots contains a serine proteinase that hydrolyzes a chromogenic peptide substrate Glp-Ala-Ala-Leu-pNA optimally at pH 8.0. Maximal activity of the proteinase in the roots is attained in April, at the beginning of plant development after the winter period. The protease was isolated by ammonium sulfate precipitation of the root extract followed by affinity chromatography on a Sepharose-Ala-Ala-Leu-mrp and gel filtration on Superose 6R performed in FPLC regime. Pure serine proteinase named taraxalisin was inactivated by specific inhibitors of serine proteinases, diisopropylfluorophosphate (DFP) and phenylmethylsulfonylfluoride (PMSF). Its molecular mass is 67 kDa and p
I 4.5. pH stability range is 6–9 in the presence of 2 mM Ca
2+, temperature optimum is at 40°C;
K
m=0.37±0.06 mM. The substrate specificity of taraxalisin towards synthetic peptides and insulin B-chain is comparable with that of two other subtilisin-like serine proteinases, cucumisin and macluralisin. The taraxalisin N-terminal sequence traced for 15 residues revealed 40% coinciding residues when aligned with that of subtilisin Carlsberg. |
| doi_str_mv | 10.1016/S0014-5793(98)01243-5 |
| format | Article |
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I 4.5. pH stability range is 6–9 in the presence of 2 mM Ca
2+, temperature optimum is at 40°C;
K
m=0.37±0.06 mM. The substrate specificity of taraxalisin towards synthetic peptides and insulin B-chain is comparable with that of two other subtilisin-like serine proteinases, cucumisin and macluralisin. The taraxalisin N-terminal sequence traced for 15 residues revealed 40% coinciding residues when aligned with that of subtilisin Carlsberg.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)01243-5</identifier><identifier>PMID: 9824298</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Asteraceae - enzymology ; Cattle ; DFP, diisopropylfluorophosphate ; EGd, l-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane ; Enzyme Activation ; Glp, pyroglutamyl ; Molecular Sequence Data ; Molecular Weight ; mrp, morpholine residue ; Plant Proteins - chemistry ; Plant Proteins - isolation & purification ; Plant Proteins - metabolism ; Plant Roots ; Plant subtilisin ; PMSF, phenylmethylsulfonylfluoride ; pNA, p-nitroanilide ; Sequence Homology, Amino Acid ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - isolation & purification ; Serine Endopeptidases - metabolism ; Serine proteinase ; Substrate Specificity ; Taraxacum officinale proteinase ; Taraxalisin</subject><ispartof>FEBS letters, 1998-10, Vol.437 (3), p.237-240</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 437 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3875-a68e1fd94930d860f8833a640984990f6c55c828e523e49b0fe846398db983933</citedby><cites>FETCH-LOGICAL-c3875-a68e1fd94930d860f8833a640984990f6c55c828e523e49b0fe846398db983933</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2901243-5$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579398012435$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27903,27904,45553,45554,46387,46811,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9824298$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rudenskaya, G.N.</creatorcontrib><creatorcontrib>Bogacheva, A.M.</creatorcontrib><creatorcontrib>Preusser, A.</creatorcontrib><creatorcontrib>Kuznetsova, A.V.</creatorcontrib><creatorcontrib>Dunaevsky, Ya.E.</creatorcontrib><creatorcontrib>Golovkin, B.N.</creatorcontrib><creatorcontrib>Stepanov, V.M.</creatorcontrib><title>Taraxalisin – a serine proteinase from dandelion Taraxacum officinale Webb s.l</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Latex of dandelion roots contains a serine proteinase that hydrolyzes a chromogenic peptide substrate Glp-Ala-Ala-Leu-pNA optimally at pH 8.0. Maximal activity of the proteinase in the roots is attained in April, at the beginning of plant development after the winter period. The protease was isolated by ammonium sulfate precipitation of the root extract followed by affinity chromatography on a Sepharose-Ala-Ala-Leu-mrp and gel filtration on Superose 6R performed in FPLC regime. Pure serine proteinase named taraxalisin was inactivated by specific inhibitors of serine proteinases, diisopropylfluorophosphate (DFP) and phenylmethylsulfonylfluoride (PMSF). Its molecular mass is 67 kDa and p
I 4.5. pH stability range is 6–9 in the presence of 2 mM Ca
2+, temperature optimum is at 40°C;
K
m=0.37±0.06 mM. The substrate specificity of taraxalisin towards synthetic peptides and insulin B-chain is comparable with that of two other subtilisin-like serine proteinases, cucumisin and macluralisin. The taraxalisin N-terminal sequence traced for 15 residues revealed 40% coinciding residues when aligned with that of subtilisin Carlsberg.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Asteraceae - enzymology</subject><subject>Cattle</subject><subject>DFP, diisopropylfluorophosphate</subject><subject>EGd, l-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane</subject><subject>Enzyme Activation</subject><subject>Glp, pyroglutamyl</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>mrp, morpholine residue</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Roots</subject><subject>Plant subtilisin</subject><subject>PMSF, phenylmethylsulfonylfluoride</subject><subject>pNA, p-nitroanilide</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - isolation & purification</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Serine proteinase</subject><subject>Substrate Specificity</subject><subject>Taraxacum officinale proteinase</subject><subject>Taraxalisin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1OGzEQxy1URAPtI0TyqSqHBXvt3cycqhbxJUUCCaoeLa93LBntR2onBW68A2_Ik7DJRrnSkzX-f8zox9hUihMpZHl6J4TUWTFD9R3hWMhcq6zYYxMJM5UpXcInNtlZPrPDlB7EMIPEA3aAkOscYcJu7220T7YJKXT87eWVW54oho74IvZLCp1NxH3sW17brqYm9B0fI27V8t774AZPQ_wPVRVPJ80Xtu9tk-jr9j1ivy_O78-usvnN5fXZz3nmFMyKzJZA0teoUYkaSuEBlLKlFggaUfjSFYWDHKjIFWmshCfQpUKoKwSFSh2xb2PvcOffFaWlaUNy1DS2o36VzEyIEgDlYCxGo4t9SpG8WcTQ2vhspDBrkmZD0qwxGQSzIWmKITfdLlhVLdW71BbdoF-N-mNo6Pn_Ss3F-a98o6wFhM33etWPsYoGYP8CRZNcoM5RHSK5pan78MGx7yPHlj8</recordid><startdate>19981023</startdate><enddate>19981023</enddate><creator>Rudenskaya, G.N.</creator><creator>Bogacheva, A.M.</creator><creator>Preusser, A.</creator><creator>Kuznetsova, A.V.</creator><creator>Dunaevsky, Ya.E.</creator><creator>Golovkin, B.N.</creator><creator>Stepanov, V.M.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19981023</creationdate><title>Taraxalisin – a serine proteinase from dandelion Taraxacum officinale Webb s.l</title><author>Rudenskaya, G.N. ; Bogacheva, A.M. ; Preusser, A. ; Kuznetsova, A.V. ; Dunaevsky, Ya.E. ; Golovkin, B.N. ; Stepanov, V.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3875-a68e1fd94930d860f8833a640984990f6c55c828e523e49b0fe846398db983933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Asteraceae - enzymology</topic><topic>Cattle</topic><topic>DFP, diisopropylfluorophosphate</topic><topic>EGd, l-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane</topic><topic>Enzyme Activation</topic><topic>Glp, pyroglutamyl</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>mrp, morpholine residue</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Roots</topic><topic>Plant subtilisin</topic><topic>PMSF, phenylmethylsulfonylfluoride</topic><topic>pNA, p-nitroanilide</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - isolation & purification</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Serine proteinase</topic><topic>Substrate Specificity</topic><topic>Taraxacum officinale proteinase</topic><topic>Taraxalisin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rudenskaya, G.N.</creatorcontrib><creatorcontrib>Bogacheva, A.M.</creatorcontrib><creatorcontrib>Preusser, A.</creatorcontrib><creatorcontrib>Kuznetsova, A.V.</creatorcontrib><creatorcontrib>Dunaevsky, Ya.E.</creatorcontrib><creatorcontrib>Golovkin, B.N.</creatorcontrib><creatorcontrib>Stepanov, V.M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rudenskaya, G.N.</au><au>Bogacheva, A.M.</au><au>Preusser, A.</au><au>Kuznetsova, A.V.</au><au>Dunaevsky, Ya.E.</au><au>Golovkin, B.N.</au><au>Stepanov, V.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Taraxalisin – a serine proteinase from dandelion Taraxacum officinale Webb s.l</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-10-23</date><risdate>1998</risdate><volume>437</volume><issue>3</issue><spage>237</spage><epage>240</epage><pages>237-240</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Latex of dandelion roots contains a serine proteinase that hydrolyzes a chromogenic peptide substrate Glp-Ala-Ala-Leu-pNA optimally at pH 8.0. Maximal activity of the proteinase in the roots is attained in April, at the beginning of plant development after the winter period. The protease was isolated by ammonium sulfate precipitation of the root extract followed by affinity chromatography on a Sepharose-Ala-Ala-Leu-mrp and gel filtration on Superose 6R performed in FPLC regime. Pure serine proteinase named taraxalisin was inactivated by specific inhibitors of serine proteinases, diisopropylfluorophosphate (DFP) and phenylmethylsulfonylfluoride (PMSF). Its molecular mass is 67 kDa and p
I 4.5. pH stability range is 6–9 in the presence of 2 mM Ca
2+, temperature optimum is at 40°C;
K
m=0.37±0.06 mM. The substrate specificity of taraxalisin towards synthetic peptides and insulin B-chain is comparable with that of two other subtilisin-like serine proteinases, cucumisin and macluralisin. The taraxalisin N-terminal sequence traced for 15 residues revealed 40% coinciding residues when aligned with that of subtilisin Carlsberg.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9824298</pmid><doi>10.1016/S0014-5793(98)01243-5</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1998-10, Vol.437 (3), p.237-240 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70068891 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Asteraceae - enzymology Cattle DFP, diisopropylfluorophosphate EGd, l-trans-epoxysuccinyl-leucylamido-(4-guanidino)butane Enzyme Activation Glp, pyroglutamyl Molecular Sequence Data Molecular Weight mrp, morpholine residue Plant Proteins - chemistry Plant Proteins - isolation & purification Plant Proteins - metabolism Plant Roots Plant subtilisin PMSF, phenylmethylsulfonylfluoride pNA, p-nitroanilide Sequence Homology, Amino Acid Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Serine proteinase Substrate Specificity Taraxacum officinale proteinase Taraxalisin |
| title | Taraxalisin – a serine proteinase from dandelion Taraxacum officinale Webb s.l |
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