Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes
Thirteen Drosophila Adh variants have been characterized with respect to gene expression, substrate preference, thermostability, and specific activity. The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, A...
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| Veröffentlicht in: | Biochemical genetics 1984-02, Vol.22 (1/2), p.153-168 |
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| container_end_page | 168 |
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| container_title | Biochemical genetics |
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| creator | Chambers, G.K Wilks, A.V Gibson, J.B |
| description | Thirteen Drosophila Adh variants have been characterized with respect to gene expression, substrate preference, thermostability, and specific activity. The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product. |
| doi_str_mv | 10.1007/BF00499295 |
| format | Article |
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The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.</description><identifier>ISSN: 0006-2928</identifier><identifier>EISSN: 1573-4927</identifier><identifier>DOI: 10.1007/BF00499295</identifier><identifier>PMID: 6370229</identifier><identifier>CODEN: BIGEBA</identifier><language>eng</language><publisher>New York, NY: Plenum Press</publisher><subject>Alcohol Dehydrogenase ; Alcohol Oxidoreductases - genetics ; Alcohol Oxidoreductases - metabolism ; Animals ; Biological and medical sciences ; Classical genetics, quantitative genetics, hybrids ; Drosophila - enzymology ; Drosophila - genetics ; Fundamental and applied biological sciences. Psychology ; gene expression ; Genetic Variation ; Genetics of eukaryotes. 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The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.</description><subject>Alcohol Dehydrogenase</subject><subject>Alcohol Oxidoreductases - genetics</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Classical genetics, quantitative genetics, hybrids</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>Genetic Variation</subject><subject>Genetics of eukaryotes. Biological and molecular evolution</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>0006-2928</issn><issn>1573-4927</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1P3DAQhi1ERRfKhTsiB9RDpbRjO_46Fgq0EhKHlko9RY49Ia6SeGtnD8uvr9tdwckav49ezTyEnFH4SAHUp6tbgMYYZsQBWVGheN0Ypg7JCgBkzQzTb8lxzr_LaKBpjsiR5AoYMyvy66dNwS4hzlWYq2XAqgvRDTgFZ8dqneIa0xIwV7H_n35JMcf1EEZb2dHFIY6Vx2HrU3zC2WYsv2N83k6Y35E3vR0znu7fE_J4e_Pj-mt9_3D37frzfe04F0ttuGis8BR0Z7xmXlLuvWXaO2Wc76EX1Ck0BqVuRKc7DWioto1XoDrpHD8h73e9Zdk_G8xLO4XscBztjHGTW02BaaFlAT_sQFduyAn7dp3CZNO2pdD-89i-eizw-b51003oX9C9uJJf7nObi6k-2dmF_IIZCY2SvGAXO6y3sbVPqSCP3xlQDkyUFin4X59Xg-k</recordid><startdate>198402</startdate><enddate>198402</enddate><creator>Chambers, G.K</creator><creator>Wilks, A.V</creator><creator>Gibson, J.B</creator><general>Plenum Press</general><scope>FBQ</scope><scope>IQODW</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>198402</creationdate><title>Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes</title><author>Chambers, G.K ; Wilks, A.V ; Gibson, J.B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-9354a5d108b9d82d613dda28dc79cdf0f51c7e99e6845b8b80e918a4d707b6cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Alcohol Dehydrogenase</topic><topic>Alcohol Oxidoreductases - genetics</topic><topic>Alcohol Oxidoreductases - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Classical genetics, quantitative genetics, hybrids</topic><topic>Drosophila - enzymology</topic><topic>Drosophila - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>Genetic Variation</topic><topic>Genetics of eukaryotes. 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The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.</abstract><cop>New York, NY</cop><pub>Plenum Press</pub><pmid>6370229</pmid><doi>10.1007/BF00499295</doi><tpages>16</tpages></addata></record> |
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| ispartof | Biochemical genetics, 1984-02, Vol.22 (1/2), p.153-168 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Alcohol Dehydrogenase Alcohol Oxidoreductases - genetics Alcohol Oxidoreductases - metabolism Animals Biological and medical sciences Classical genetics, quantitative genetics, hybrids Drosophila - enzymology Drosophila - genetics Fundamental and applied biological sciences. Psychology gene expression Genetic Variation Genetics of eukaryotes. Biological and molecular evolution Isoenzymes - genetics Isoenzymes - metabolism Substrate Specificity Temperature |
| title | Variation in the biochemical properties of the Drosophila alcohol dehydrogenase allozymes |
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