Esterase-6 allozymes: biochemical studies of two common and one rare variant in Drosophila melanogaster
The biochemical properties of three allozymes coded by the Est-6 locus, two common forms (EST-6S and EST-6F) and one rare form (EST-6VF), were studied. The results show the existence of differences in isoelectric point, activity, activation energy, Km, and temperature coefficient among the three var...
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| Veröffentlicht in: | Biochemical genetics 1983-02, Vol.21 (1-2), p.191-197 |
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| container_title | Biochemical genetics |
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| creator | Costa, R Nigro, L Danieli, G A |
| description | The biochemical properties of three allozymes coded by the Est-6 locus, two common forms (EST-6S and EST-6F) and one rare form (EST-6VF), were studied. The results show the existence of differences in isoelectric point, activity, activation energy, Km, and temperature coefficient among the three variants, especially between the two common forms and the one rare form. The specific activity of the rare enzymatic variant seems to be less affected by temperature variation. The possible significance of these findings in relation to the mechanism of reproduction is briefly discussed. |
| doi_str_mv | 10.1007/BF02395403 |
| format | Article |
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The results show the existence of differences in isoelectric point, activity, activation energy, Km, and temperature coefficient among the three variants, especially between the two common forms and the one rare form. The specific activity of the rare enzymatic variant seems to be less affected by temperature variation. The possible significance of these findings in relation to the mechanism of reproduction is briefly discussed.</description><identifier>ISSN: 0006-2928</identifier><identifier>DOI: 10.1007/BF02395403</identifier><identifier>PMID: 6404245</identifier><language>eng</language><publisher>United States</publisher><subject>Alleles ; Animals ; Carboxylesterase ; Carboxylic Ester Hydrolases - genetics ; Drosophila melanogaster - enzymology ; Drosophila melanogaster - genetics ; Drosophila Proteins ; Genetic Variation ; Homozygote ; Isoenzymes - genetics ; Isoenzymes - metabolism ; Kinetics ; Thermodynamics</subject><ispartof>Biochemical genetics, 1983-02, Vol.21 (1-2), p.191-197</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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/6404245$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Costa, R</creatorcontrib><creatorcontrib>Nigro, L</creatorcontrib><creatorcontrib>Danieli, G A</creatorcontrib><title>Esterase-6 allozymes: biochemical studies of two common and one rare variant in Drosophila melanogaster</title><title>Biochemical genetics</title><addtitle>Biochem Genet</addtitle><description>The biochemical properties of three allozymes coded by the Est-6 locus, two common forms (EST-6S and EST-6F) and one rare form (EST-6VF), were studied. The results show the existence of differences in isoelectric point, activity, activation energy, Km, and temperature coefficient among the three variants, especially between the two common forms and the one rare form. The specific activity of the rare enzymatic variant seems to be less affected by temperature variation. The possible significance of these findings in relation to the mechanism of reproduction is briefly discussed.</description><subject>Alleles</subject><subject>Animals</subject><subject>Carboxylesterase</subject><subject>Carboxylic Ester Hydrolases - genetics</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila Proteins</subject><subject>Genetic Variation</subject><subject>Homozygote</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Thermodynamics</subject><issn>0006-2928</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotkDFPwzAUhD2ASiks7Eie2ALP9ksas0GhgFSJBeboNXlpg-I42Amo_HqK6HQ66dPd6YS4UHCtAOY390vQxqYI5khMASBLtNX5iTiN8WNvLSBOxCRDQI3pVGwe48CBIieZpLb1PzvH8VauG19u2TUltTIOY9VwlL6Ww7eXpXfOd5K6SvqOZaDA8otCQ90gm04-BB99v21ako5b6vyG_hrOxHFNbeTzg87E-_LxbfGcrF6fXhZ3q6RXWg2JIrMmxQa1rXWm8znliJgqzlIDwFYjEzHbqgSyaVVjpRGoLA3kualVambi6j-3D_5z5DgUroklt_sl7MdY5IBmbhH34OUBHNeOq6IPjaOwKw7PmF9yeWMh</recordid><startdate>198302</startdate><enddate>198302</enddate><creator>Costa, R</creator><creator>Nigro, L</creator><creator>Danieli, G A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>198302</creationdate><title>Esterase-6 allozymes: biochemical studies of two common and one rare variant in Drosophila melanogaster</title><author>Costa, R ; Nigro, L ; Danieli, G A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p121t-1a3ba1e3429f26287a844451e65300e924eaaee9dc0a95df4d240acc30883f153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Alleles</topic><topic>Animals</topic><topic>Carboxylesterase</topic><topic>Carboxylic Ester Hydrolases - genetics</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila Proteins</topic><topic>Genetic Variation</topic><topic>Homozygote</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Costa, R</creatorcontrib><creatorcontrib>Nigro, L</creatorcontrib><creatorcontrib>Danieli, G A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Costa, R</au><au>Nigro, L</au><au>Danieli, G A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Esterase-6 allozymes: biochemical studies of two common and one rare variant in Drosophila melanogaster</atitle><jtitle>Biochemical genetics</jtitle><addtitle>Biochem Genet</addtitle><date>1983-02</date><risdate>1983</risdate><volume>21</volume><issue>1-2</issue><spage>191</spage><epage>197</epage><pages>191-197</pages><issn>0006-2928</issn><abstract>The biochemical properties of three allozymes coded by the Est-6 locus, two common forms (EST-6S and EST-6F) and one rare form (EST-6VF), were studied. The results show the existence of differences in isoelectric point, activity, activation energy, Km, and temperature coefficient among the three variants, especially between the two common forms and the one rare form. The specific activity of the rare enzymatic variant seems to be less affected by temperature variation. The possible significance of these findings in relation to the mechanism of reproduction is briefly discussed.</abstract><cop>United States</cop><pmid>6404245</pmid><doi>10.1007/BF02395403</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical genetics, 1983-02, Vol.21 (1-2), p.191-197 |
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| language | eng |
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| source | MEDLINE; SpringerLink Journals |
| subjects | Alleles Animals Carboxylesterase Carboxylic Ester Hydrolases - genetics Drosophila melanogaster - enzymology Drosophila melanogaster - genetics Drosophila Proteins Genetic Variation Homozygote Isoenzymes - genetics Isoenzymes - metabolism Kinetics Thermodynamics |
| title | Esterase-6 allozymes: biochemical studies of two common and one rare variant in Drosophila melanogaster |
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