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- W24939948 abstract "ABSTRACT. δ-Aminolevulinate dehydratase isolated from fetal liver and a hepatoma has been compared to the enzyme from adult liver. The fetal liver enzyme is less stable to denaturation by heat and is catalytically more efficient than the enzyme from adult liver. The enzyme from a fast growing hepatoma has the same properties as the enzyme from fetal liver. The enzymes from all three tissue sources are similar in molecular size, electrophoretic mobility, apparent K m for the substrate, δ-aminolevulinic acid, number of active sites, and pattern of peptides released by trypsin. These results indicate that the cellular mechanism controlling the structure of δ-aminolevulinate dehydratase in fetal liver is expressed again in the hepatoma and that a combined genetic-biochemical approach can provide insight into this mechanism of regulation." @default.
- W24939948 created "2016-06-24" @default.
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- W24939948 date "1975-01-01" @default.
- W24939948 modified "2023-09-27" @default.
- W24939948 title "GENETIC CONTROL OF δ-AMINOLEVULINATE DEHYDRATASE IN ADULT LIVER, FETAL LIVER, AND A HEPATOMA OF INBRED MICE" @default.
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- W24939948 doi "https://doi.org/10.1016/b978-0-12-472703-8.50060-3" @default.
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