Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid
A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 5...
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| Veröffentlicht in: | Planta 1995, Vol.196 (1), p.174-179 |
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| creator | Rudenskaya, G.N Bogdanova, E.A Revina, L.P Golovkin, B.N Stepanov, V.M |
| description | A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom. |
| doi_str_mv | 10.1007/BF00193231 |
| format | Article |
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Schneid</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Rudenskaya, G.N ; Bogdanova, E.A ; Revina, L.P ; Golovkin, B.N ; Stepanov, V.M</creator><creatorcontrib>Rudenskaya, G.N ; Bogdanova, E.A ; Revina, L.P ; Golovkin, B.N ; Stepanov, V.M</creatorcontrib><description>A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/BF00193231</identifier><identifier>PMID: 7767235</identifier><language>eng</language><publisher>Germany: Springer-Verlag</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Amino acids ; Bacitracin ; Biotechnology ; characterization ; chemical composition ; Chromatography, Affinity ; Chromatography, Gel ; enzyme activity ; enzyme inhibitors ; Enzymes ; Fruit - enzymology ; fruits ; glycoproteins ; Glycoproteins - chemistry ; Insulin ; isolation ; Maclura pomifera ; Molecular Sequence Data ; n-terminal sequence ; phylogeny ; Plant biochemistry ; Plant Proteins - chemistry ; Plant Proteins - isolation & purification ; Plants ; Plants - enzymology ; Sequence Homology, Amino Acid ; Serine Endopeptidases - chemistry ; Serine Endopeptidases - isolation & purification ; serine proteinases ; Sorbents ; Soybeans ; Substrate Specificity ; substrates ; subtilisin ; Subtilisins - chemistry ; Subtilisins - isolation & purification ; temperature ; Trypsin inhibitors ; Ungulates</subject><ispartof>Planta, 1995, Vol.196 (1), p.174-179</ispartof><rights>Springer-Verlag Berlin Heidelberg 1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c328t-690261588aa09b97f6379c6486a688c628ddef4381db4fa9c0f13d430711359f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23383362$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23383362$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,4010,27902,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7767235$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rudenskaya, G.N</creatorcontrib><creatorcontrib>Bogdanova, E.A</creatorcontrib><creatorcontrib>Revina, L.P</creatorcontrib><creatorcontrib>Golovkin, B.N</creatorcontrib><creatorcontrib>Stepanov, V.M</creatorcontrib><title>Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid</title><title>Planta</title><addtitle>Planta</addtitle><description>A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Bacitracin</subject><subject>Biotechnology</subject><subject>characterization</subject><subject>chemical composition</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>enzyme activity</subject><subject>enzyme inhibitors</subject><subject>Enzymes</subject><subject>Fruit - enzymology</subject><subject>fruits</subject><subject>glycoproteins</subject><subject>Glycoproteins - chemistry</subject><subject>Insulin</subject><subject>isolation</subject><subject>Maclura pomifera</subject><subject>Molecular Sequence Data</subject><subject>n-terminal sequence</subject><subject>phylogeny</subject><subject>Plant biochemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plants</subject><subject>Plants - enzymology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - isolation & purification</subject><subject>serine proteinases</subject><subject>Sorbents</subject><subject>Soybeans</subject><subject>Substrate Specificity</subject><subject>substrates</subject><subject>subtilisin</subject><subject>Subtilisins - chemistry</subject><subject>Subtilisins - isolation & purification</subject><subject>temperature</subject><subject>Trypsin inhibitors</subject><subject>Ungulates</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkN9LwzAQx4Moc05ffBf7JCp0Jrk2Px51OBUminPPJWsTzWibmbQP_vdGNjYIl4PP547ji9A5wWOCMb97mGJMJFAgB2hIMqApxZk4REOMY48l5MfoJIRVtDLgfIAGnDNOIR-i91dV1r1XtQ22TVOVBO1tq5O1d522rQo6Md41sfS2C4kzyXYgWbvGGh2b6w9lxjfJvPxuta1O0ZFRddBn23-EFtPHz8lzOnt7epncz9ISqOhSJjFlJBdCKSyXkhsGXJYsE0wxIUpGRVVpk4Eg1TIzSpbYEKgywJwQyKWBEbra7I2X_vQ6dEVjQ6nrWrXa9aHgnErGGYvi7UYsvQvBa1OsvW2U_y0ILv7jK_bxRfliu7VfNrraqdu89nwVOud3mAIIAEYjv9xwo1yhvrwNxWJOMQFMRcTx_QF3b3qp</recordid><startdate>1995</startdate><enddate>1995</enddate><creator>Rudenskaya, G.N</creator><creator>Bogdanova, E.A</creator><creator>Revina, L.P</creator><creator>Golovkin, B.N</creator><creator>Stepanov, V.M</creator><general>Springer-Verlag</general><scope>FBQ</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>1995</creationdate><title>Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid</title><author>Rudenskaya, G.N ; Bogdanova, E.A ; Revina, L.P ; Golovkin, B.N ; Stepanov, V.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c328t-690261588aa09b97f6379c6486a688c628ddef4381db4fa9c0f13d430711359f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Amino acids</topic><topic>Bacitracin</topic><topic>Biotechnology</topic><topic>characterization</topic><topic>chemical composition</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>enzyme activity</topic><topic>enzyme inhibitors</topic><topic>Enzymes</topic><topic>Fruit - enzymology</topic><topic>fruits</topic><topic>glycoproteins</topic><topic>Glycoproteins - chemistry</topic><topic>Insulin</topic><topic>isolation</topic><topic>Maclura pomifera</topic><topic>Molecular Sequence Data</topic><topic>n-terminal sequence</topic><topic>phylogeny</topic><topic>Plant biochemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plants</topic><topic>Plants - enzymology</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases - chemistry</topic><topic>Serine Endopeptidases - isolation & purification</topic><topic>serine proteinases</topic><topic>Sorbents</topic><topic>Soybeans</topic><topic>Substrate Specificity</topic><topic>substrates</topic><topic>subtilisin</topic><topic>Subtilisins - chemistry</topic><topic>Subtilisins - isolation & purification</topic><topic>temperature</topic><topic>Trypsin inhibitors</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rudenskaya, G.N</creatorcontrib><creatorcontrib>Bogdanova, E.A</creatorcontrib><creatorcontrib>Revina, L.P</creatorcontrib><creatorcontrib>Golovkin, B.N</creatorcontrib><creatorcontrib>Stepanov, V.M</creatorcontrib><collection>AGRIS</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>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rudenskaya, G.N</au><au>Bogdanova, E.A</au><au>Revina, L.P</au><au>Golovkin, B.N</au><au>Stepanov, V.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid</atitle><jtitle>Planta</jtitle><addtitle>Planta</addtitle><date>1995</date><risdate>1995</risdate><volume>196</volume><issue>1</issue><spage>174</spage><epage>179</epage><pages>174-179</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><abstract>A serine proteinase was isolated from fruits of Maclura pomifera (Raf.) Schneid. by affinity chromatography on bacitracin-containing sorbents and gel-filtration. The enzyme, named macluralisin, is a glycoprotein with a molecular mass of 65 kDa; its protein moiety corresponds to a molecular mass of 50 kDa. The substrate specificity of macluralisin towards synthetic peptides and insulin B-chain is similar to that of cucumisin, a subtilisin-like proteinase from melon fruit. The enzyme is completely inhibited by diisopropylfluorophosphate. Its amino-acid composition resembles that of a serine proteinase isolated from the Cucurbitaceae. The N-terminal sequence has 33% of its residues identical to those of the sequence of fungal subtilisin-like proteinase K. Hence, Maclura pomifera serine proteinase belongs to the subtilisin family, which seems to be broadly distributed in the plant kingdom.</abstract><cop>Germany</cop><pub>Springer-Verlag</pub><pmid>7767235</pmid><doi>10.1007/BF00193231</doi><tpages>6</tpages></addata></record> |
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| source | Jstor Complete Legacy; MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Amino Acid Sequence amino acid sequences Amino acids Bacitracin Biotechnology characterization chemical composition Chromatography, Affinity Chromatography, Gel enzyme activity enzyme inhibitors Enzymes Fruit - enzymology fruits glycoproteins Glycoproteins - chemistry Insulin isolation Maclura pomifera Molecular Sequence Data n-terminal sequence phylogeny Plant biochemistry Plant Proteins - chemistry Plant Proteins - isolation & purification Plants Plants - enzymology Sequence Homology, Amino Acid Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification serine proteinases Sorbents Soybeans Substrate Specificity substrates subtilisin Subtilisins - chemistry Subtilisins - isolation & purification temperature Trypsin inhibitors Ungulates |
| title | Macluralisin--a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid |
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