Limited proteolysis of tryptophanyl-tRNA synthetase from beef pancreas
Treatment of purified tryptophanyl‐tRNA synthetase with either chymotrypsin, papain, subtilisin or elastase converts all the enzyme into a high‐molecular‐weight intermediate. This protease‐resistant core molecule has the same dimeric structure as the native protein and possesses the ability to bind...
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| Veröffentlicht in: | European journal of biochemistry 1976-01, Vol.61 (1), p.139-146 |
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| container_end_page | 146 |
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| container_title | European journal of biochemistry |
| container_volume | 61 |
| creator | Epely, S Gros, C Labouesse, J Lemaire, G |
| description | Treatment of purified tryptophanyl‐tRNA synthetase with either chymotrypsin, papain, subtilisin or elastase converts all the enzyme into a high‐molecular‐weight intermediate. This protease‐resistant core molecule has the same dimeric structure as the native protein and possesses the ability to bind substrates (tryptophan, ATP and tRNATrp) but is catalytically inactive.
The monomer molecular weight of the protease‐treated enzyme is 39000 compared to 54000 for the intact molecule. Chemical studies indicate that proteases excise the amino‐terminal part of the polypeptide chain. It has been demonstrated previously that removal of a 13000‐dalton fragment from the amino‐terminal region of the tryptophanyl‐tRNA synthetase converts the native enzyme to another active form. Cleavage of 20 additional amino acids produces the inactive protease‐resistant core. |
| doi_str_mv | 10.1111/j.1432-1033.1976.tb10004.x |
| format | Article |
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The monomer molecular weight of the protease‐treated enzyme is 39000 compared to 54000 for the intact molecule. Chemical studies indicate that proteases excise the amino‐terminal part of the polypeptide chain. It has been demonstrated previously that removal of a 13000‐dalton fragment from the amino‐terminal region of the tryptophanyl‐tRNA synthetase converts the native enzyme to another active form. Cleavage of 20 additional amino acids produces the inactive protease‐resistant core.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1976.tb10004.x</identifier><identifier>PMID: 1245179</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acids - analysis ; Amino Acyl-tRNA Synthetases - analysis ; animal science ; Animals ; Cattle ; Chymotrypsin ; Kinetics ; livestock ; Macromolecular Substances ; Molecular Weight ; Pancreas - enzymology ; Pancreatic Elastase ; Papain ; Peptide Fragments - analysis ; Subtilisins ; Tryptophan-tRNA Ligase - analysis ; Tryptophan-tRNA Ligase - metabolism ; zoology</subject><ispartof>European journal of biochemistry, 1976-01, Vol.61 (1), p.139-146</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4469-8a861716bb30fd750855af34bf33700283d5a8c74f00b877db033e16472bd4073</citedby><cites>FETCH-LOGICAL-c4469-8a861716bb30fd750855af34bf33700283d5a8c74f00b877db033e16472bd4073</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1245179$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Epely, S</creatorcontrib><creatorcontrib>Gros, C</creatorcontrib><creatorcontrib>Labouesse, J</creatorcontrib><creatorcontrib>Lemaire, G</creatorcontrib><title>Limited proteolysis of tryptophanyl-tRNA synthetase from beef pancreas</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Treatment of purified tryptophanyl‐tRNA synthetase with either chymotrypsin, papain, subtilisin or elastase converts all the enzyme into a high‐molecular‐weight intermediate. This protease‐resistant core molecule has the same dimeric structure as the native protein and possesses the ability to bind substrates (tryptophan, ATP and tRNATrp) but is catalytically inactive.
The monomer molecular weight of the protease‐treated enzyme is 39000 compared to 54000 for the intact molecule. Chemical studies indicate that proteases excise the amino‐terminal part of the polypeptide chain. It has been demonstrated previously that removal of a 13000‐dalton fragment from the amino‐terminal region of the tryptophanyl‐tRNA synthetase converts the native enzyme to another active form. Cleavage of 20 additional amino acids produces the inactive protease‐resistant core.</description><subject>Amino Acids - analysis</subject><subject>Amino Acyl-tRNA Synthetases - analysis</subject><subject>animal science</subject><subject>Animals</subject><subject>Cattle</subject><subject>Chymotrypsin</subject><subject>Kinetics</subject><subject>livestock</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>Pancreas - enzymology</subject><subject>Pancreatic Elastase</subject><subject>Papain</subject><subject>Peptide Fragments - analysis</subject><subject>Subtilisins</subject><subject>Tryptophan-tRNA Ligase - analysis</subject><subject>Tryptophan-tRNA Ligase - metabolism</subject><subject>zoology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkEFP3DAQha2qFWwpP6Ei6oFb0pnYsR0uCBDbVlqBVOBs2YkNWSWb1PYK8u-bKKty7lzm8N68mfkI-YaQ4VTftxkymqcIlGZYCp5FgwDAsrcPZPVP-khWAMjSvCz4Mfkcwnby8JKLI3KEOStQlCuy3jRdE22dDL6Ptm_H0ISkd0n04xD74UXvxjaNv--ukjDu4ouNOtjE-b5LjLUuGfSu8laHL-ST022wp4d-Qp7Wt483P9PN_Y9fN1ebtGKMl6nUkqNAbgwFV4sCZFFoR5lxlAqAXNK60LISzAEYKURtpj8sciZyUzMQ9IScL7nTuX_2NkTVNaGybat3tt8HJSmClDlMxovFWPk-BG-dGnzTaT8qBDVDVFs1k1IzKTVDVAeI6m0a_nrYsjedrd9HF2qTfrnor01rx_9IVuvb6wekc8LZkuB0r_Szb4J6esgBKVBAKCSnfwGlHYoe</recordid><startdate>197601</startdate><enddate>197601</enddate><creator>Epely, S</creator><creator>Gros, C</creator><creator>Labouesse, J</creator><creator>Lemaire, G</creator><general>Blackwell Publishing Ltd</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>197601</creationdate><title>Limited proteolysis of tryptophanyl-tRNA synthetase from beef pancreas</title><author>Epely, S ; Gros, C ; Labouesse, J ; Lemaire, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4469-8a861716bb30fd750855af34bf33700283d5a8c74f00b877db033e16472bd4073</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Amino Acids - analysis</topic><topic>Amino Acyl-tRNA Synthetases - analysis</topic><topic>animal science</topic><topic>Animals</topic><topic>Cattle</topic><topic>Chymotrypsin</topic><topic>Kinetics</topic><topic>livestock</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>Pancreas - enzymology</topic><topic>Pancreatic Elastase</topic><topic>Papain</topic><topic>Peptide Fragments - analysis</topic><topic>Subtilisins</topic><topic>Tryptophan-tRNA Ligase - analysis</topic><topic>Tryptophan-tRNA Ligase - metabolism</topic><topic>zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Epely, S</creatorcontrib><creatorcontrib>Gros, C</creatorcontrib><creatorcontrib>Labouesse, J</creatorcontrib><creatorcontrib>Lemaire, G</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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Epely, S</au><au>Gros, C</au><au>Labouesse, J</au><au>Lemaire, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Limited proteolysis of tryptophanyl-tRNA synthetase from beef pancreas</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1976-01</date><risdate>1976</risdate><volume>61</volume><issue>1</issue><spage>139</spage><epage>146</epage><pages>139-146</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Treatment of purified tryptophanyl‐tRNA synthetase with either chymotrypsin, papain, subtilisin or elastase converts all the enzyme into a high‐molecular‐weight intermediate. This protease‐resistant core molecule has the same dimeric structure as the native protein and possesses the ability to bind substrates (tryptophan, ATP and tRNATrp) but is catalytically inactive.
The monomer molecular weight of the protease‐treated enzyme is 39000 compared to 54000 for the intact molecule. Chemical studies indicate that proteases excise the amino‐terminal part of the polypeptide chain. It has been demonstrated previously that removal of a 13000‐dalton fragment from the amino‐terminal region of the tryptophanyl‐tRNA synthetase converts the native enzyme to another active form. Cleavage of 20 additional amino acids produces the inactive protease‐resistant core.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1245179</pmid><doi>10.1111/j.1432-1033.1976.tb10004.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1976-01, Vol.61 (1), p.139-146 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Amino Acyl-tRNA Synthetases - analysis animal science Animals Cattle Chymotrypsin Kinetics livestock Macromolecular Substances Molecular Weight Pancreas - enzymology Pancreatic Elastase Papain Peptide Fragments - analysis Subtilisins Tryptophan-tRNA Ligase - analysis Tryptophan-tRNA Ligase - metabolism zoology |
| title | Limited proteolysis of tryptophanyl-tRNA synthetase from beef pancreas |
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