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- W52268483 abstract "Research Article1 April 1985free access Fused lacZ genes code for di-, tri- and tetra-beta-galactosidase in Escherichia coli. W. Kuchinke W. Kuchinke Search for more papers by this author B. Müller-Hill B. Müller-Hill Search for more papers by this author W. Kuchinke W. Kuchinke Search for more papers by this author B. Müller-Hill B. Müller-Hill Search for more papers by this author Author Information W. Kuchinke and B. Müller-Hill The EMBO Journal (1985)4:1067-1073https://doi.org/10.1002/j.1460-2075.1985.tb03740.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Plasmids were constructed which carry two, three or four active lacZ genes of Escherichia coli fused head-to-tail in phase. The products of these oligomeric lacZ genes are shown to be polypeptides with expected subunit mol. wts. of 230 kd (di-beta-galactosidase), 350 kd (tri-beta-galactosidase) and 460 kd (tetra-beta-galactosidase). Di-beta-galactosidase has the same enzymatic activity as the wild-type enzyme. It subunits are practically not degraded proteolytically in vivo. It aggregates predominantly to a dimer which has the same sedimentation constant as the wild-type tetrameric enzyme. Furthermore, it is more heat stable than the wild-type enzyme. Tri- and tetra-beta-galactosidase have strongly reduced enzymatic activities and are largely degraded. Our experiments lead us to propose that covalent joining of two subunits through proper gene duplication may possibly be an intermediate in the evolution of self aggregation of homo-oligomeric proteins. Previous ArticleNext Article Volume 4Issue 41 April 1985In this issue RelatedDetailsLoading ..." @default.
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- W52268483 title "Fused lacZ genes code for di-, tri- and tetra-beta-galactosidase in Escherichia coli." @default.
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- W52268483 doi "https://doi.org/10.1002/j.1460-2075.1985.tb03740.x" @default.
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