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- W2008849095 abstract "1. Triosephosphate isomerase from a variety of human tissues exhibits three catalytically active components upon starch gel electrophoresis or isoelectric focusing. 2. The three isoenzymes and relative distribution are identical in all tissues, and the multiplicity is not the result of tissue-specific variation. 3. In general, vertebrates exhibit three major triosephosphate isomerase isoenzymes; invertebrates contain one, two or three forms; and microorganisms possess only a single electrophoretic form of the enzyme. 4. The results suggest that the enzymatic multiplicity of triosephosphate isomerase is of genetic origin, and that gene duplication may have occurred in some primordial invertebrate." @default.
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- W2008849095 date "1974-12-01" @default.
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- W2008849095 title "Comparison of the electrophoretic properties of triosephosphate isomerases of various tissues and species" @default.
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- W2008849095 doi "https://doi.org/10.1016/0305-0491(74)90259-4" @default.
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