Differences in charge and kinetic properties of alcohol dehydrogenase 4 from C57BL/6 mice compared to other inbred strains are associated with a cysteine120 to arginine120 substitution.
作者： Daniel E. A. Dolney , Gabor Szalai , Michael R. Felder
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摘要: Alcohol dehydrogenase class IV (ADH4) participates in retinol metabolism and is expressed primarily ocular, digestive, reproductive tissues of the mouse. A naturally occurring genetic variant C57BL/6J mice results a faster migrating ADH4 enzyme during electrophoresis when compared to other non-C57BJ/6J strains. The C57BL/6 gene coding sequence found have two nucleotide substitutions from C3HeB/FeJ mice. substitution exon 5 encodes Arg120 instead Cys120 polypeptide; that would account for protein electrophoretic phenotype. present all published mammalian sequences but only limited number mouse residue part outer loop substrate binding pocket appears an effect on affinity several substrates.
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