Isolation of the mature subunit of delta-aminolaevulinate synthase from embryonic chick liver

We presented evidence indicating that the established procedure for purifying delta-aminolaevulinate (ALA) synthase from embryonic-chick liver yielded an enzyme with a partially degraded subunit of molecular weight 51000 [Ades & Harpe (1981) J. Biol. Chem. 256, 9329-9333]. We now report the puri...

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Veröffentlicht in:	Biochemical journal 1982-08, Vol.205 (2), p.257-263
Hauptverfasser:	Ades, I Z, Harpe, K G
Format:	Artikel
Sprache:	eng
Schlagworte:	5-aminolaevulinate synthase 5-Aminolevulinate Synthetase - isolation & purification Animals Chick Embryo chick embryos Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Isoelectric Focusing liver Mitochondria, Liver - enzymology Molecular Weight Peptide Fragments - analysis purification
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creator	Ades, I Z Harpe, K G
description	We presented evidence indicating that the established procedure for purifying delta-aminolaevulinate (ALA) synthase from embryonic-chick liver yielded an enzyme with a partially degraded subunit of molecular weight 51000 [Ades & Harpe (1981) J. Biol. Chem. 256, 9329-9333]. We now report the purification from livers of porphyric embryos of a preparation of ALA synthase which consisted primarily of a 63000-Da polypeptide and a component migrating as a smear of polypeptides with a minimum molecular weight of 52 000. Neither component could be recovered from liver mitochondria of normal embryos, where the amounts of ALA synthase were relatively low. The 52 000-Da component had been established to be the partially degraded subunit of the enzyme. Peptide-mapping analyses indicated that the 63 000- and the 52 000-Da components possessed significant structural homologies, and it was concluded that the 63 000-Da polypeptide represented the mature subunit of ALA synthase.
doi_str_mv	10.1042/bj2050257
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Biol. Chem. 256, 9329-9333]. We now report the purification from livers of porphyric embryos of a preparation of ALA synthase which consisted primarily of a 63000-Da polypeptide and a component migrating as a smear of polypeptides with a minimum molecular weight of 52 000. Neither component could be recovered from liver mitochondria of normal embryos, where the amounts of ALA synthase were relatively low. The 52 000-Da component had been established to be the partially degraded subunit of the enzyme. Peptide-mapping analyses indicated that the 63 000- and the 52 000-Da components possessed significant structural homologies, and it was concluded that the 63 000-Da polypeptide represented the mature subunit of ALA synthase.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2050257</identifier><identifier>PMID: 7138500</identifier><language>eng</language><publisher>England</publisher><subject>5-aminolaevulinate synthase ; 5-Aminolevulinate Synthetase - isolation & purification ; Animals ; Chick Embryo ; chick embryos ; Chromatography, Affinity ; Electrophoresis, Polyacrylamide Gel ; Isoelectric Focusing ; liver ; Mitochondria, Liver - enzymology ; Molecular Weight ; Peptide Fragments - analysis ; purification</subject><ispartof>Biochemical journal, 1982-08, Vol.205 (2), p.257-263</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3167-720f798db08be43f7f08624a00fbe76dc9fbada210228565f09a85f4707ca86c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1158476/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1158476/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7138500$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ades, I Z</creatorcontrib><creatorcontrib>Harpe, K G</creatorcontrib><title>Isolation of the mature subunit of delta-aminolaevulinate synthase from embryonic chick liver</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>We presented evidence indicating that the established procedure for purifying delta-aminolaevulinate (ALA) synthase from embryonic-chick liver yielded an enzyme with a partially degraded subunit of molecular weight 51000 [Ades & Harpe (1981) J. Biol. Chem. 256, 9329-9333]. We now report the purification from livers of porphyric embryos of a preparation of ALA synthase which consisted primarily of a 63000-Da polypeptide and a component migrating as a smear of polypeptides with a minimum molecular weight of 52 000. Neither component could be recovered from liver mitochondria of normal embryos, where the amounts of ALA synthase were relatively low. The 52 000-Da component had been established to be the partially degraded subunit of the enzyme. Peptide-mapping analyses indicated that the 63 000- and the 52 000-Da components possessed significant structural homologies, and it was concluded that the 63 000-Da polypeptide represented the mature subunit of ALA synthase.</description><subject>5-aminolaevulinate synthase</subject><subject>5-Aminolevulinate Synthetase - isolation & purification</subject><subject>Animals</subject><subject>Chick Embryo</subject><subject>chick embryos</subject><subject>Chromatography, Affinity</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Isoelectric Focusing</subject><subject>liver</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - analysis</subject><subject>purification</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LxDAQhoMo6_px8AcIPQkeqpM0abIXQcQvELzoUUKaJm7WNtEkXdh_bxeXRU8ehoGZh4cZXoROMFxgoOSyWRBgQBjfQVNMOZSCE7GLpkBqWtZA8D46SGkBgClQmKAJx5VgAFP09phCp7ILvgi2yHNT9CoP0RRpaAbv8nrami6rUvXOj6hZDp3zKo_Eyue5SqawMfSF6Zu4Ct7pQs-d_ig6tzTxCO1Z1SVzvOmH6PXu9uXmoXx6vn-8uX4qdYVrXnICls9E24BoDK0styBqQhWAbQyvWz2zjWoVwUCIYDWzMFOC2fFRrpWodXWIrn68n0PTm1Ybn6Pq5Gd0vYorGZSTfzfezeV7WEqMmaC8HgVnG0EMX4NJWfYuadN1ypswJMkp4bMK2L8gZlSMtTae_4A6hpSisdtrMMh1aHIb2sie_j5_S25Sqr4B03WT2w</recordid><startdate>19820801</startdate><enddate>19820801</enddate><creator>Ades, I Z</creator><creator>Harpe, K G</creator><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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19820801</creationdate><title>Isolation of the mature subunit of delta-aminolaevulinate synthase from embryonic chick liver</title><author>Ades, I Z ; Harpe, K G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3167-720f798db08be43f7f08624a00fbe76dc9fbada210228565f09a85f4707ca86c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>5-aminolaevulinate synthase</topic><topic>5-Aminolevulinate Synthetase - isolation & purification</topic><topic>Animals</topic><topic>Chick Embryo</topic><topic>chick embryos</topic><topic>Chromatography, Affinity</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Isoelectric Focusing</topic><topic>liver</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - analysis</topic><topic>purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ades, I Z</creatorcontrib><creatorcontrib>Harpe, K G</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ades, I Z</au><au>Harpe, K G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation of the mature subunit of delta-aminolaevulinate synthase from embryonic chick liver</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1982-08-01</date><risdate>1982</risdate><volume>205</volume><issue>2</issue><spage>257</spage><epage>263</epage><pages>257-263</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>We presented evidence indicating that the established procedure for purifying delta-aminolaevulinate (ALA) synthase from embryonic-chick liver yielded an enzyme with a partially degraded subunit of molecular weight 51000 [Ades & Harpe (1981) J. Biol. Chem. 256, 9329-9333]. We now report the purification from livers of porphyric embryos of a preparation of ALA synthase which consisted primarily of a 63000-Da polypeptide and a component migrating as a smear of polypeptides with a minimum molecular weight of 52 000. Neither component could be recovered from liver mitochondria of normal embryos, where the amounts of ALA synthase were relatively low. The 52 000-Da component had been established to be the partially degraded subunit of the enzyme. Peptide-mapping analyses indicated that the 63 000- and the 52 000-Da components possessed significant structural homologies, and it was concluded that the 63 000-Da polypeptide represented the mature subunit of ALA synthase.</abstract><cop>England</cop><pmid>7138500</pmid><doi>10.1042/bj2050257</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
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subjects	5-aminolaevulinate synthase 5-Aminolevulinate Synthetase - isolation & purification Animals Chick Embryo chick embryos Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Isoelectric Focusing liver Mitochondria, Liver - enzymology Molecular Weight Peptide Fragments - analysis purification
title	Isolation of the mature subunit of delta-aminolaevulinate synthase from embryonic chick liver
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