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- W1967138751 abstract "Abstract The basis for the known transient accumulation of heme precursors during fetal development was investigated by comparing the characteristics of multiple forms of the first enzyme in the heme biosynthetic pathway, δ-aminolevulinate synthetase, derived from guinea pig fetal and adult liver and adult bone marrow. The elevation of δ-aminolevulinate synthetase in fetal liver was correlated with the transient establishment of erythropoietic activity in this organ during prenatal development. Partially purified mitochondrial synthetase from fetal liver and adult bone marrow (erythroid forms) was not bound to AMP- or CoA-agarose whereas the adult hepatic (nonerythroid) synthetase was strongly bound. For the first time, it was possible to demonstrate the identity of uninduced with 3,5-dicarbethoxy-1,4-dihydrocollidine-induced δ-aminolevulinate synthetase on the basis of the ability of both enzyme preparations to bind strongly to AMP-agarose. Weak binding of the erythroid forms to AMP-and CoA-agarose was observed in the presence of high concentrations of glycine. The erythroid forms had similar K0.5's for glycine (14 m m ) in contrast to the nonerythroid form, which exhibited a K0.5 of 3 m m and showed negative cooperativity. Additional kinetic studies suggested nucleotide regulation of enzyme activity. Sodium chloride (0.4 m ) strongly inhibited the erythroid enzymes but only slightly inhibited the nonerythroid synthetase. Furthermore, the specific activities of the crude extracts of the erythroid forms were 30 to 60 times that of the uninduced hepatic nonerythroid form. The apparent molecular weights of all three forms were approximately 110,000. The only significant difference between the two erythroid forms were their rates of heat inactivation at 45 °C." @default.
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- W1967138751 date "1981-02-01" @default.
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- W1967138751 title "Evidence for erythroid and nonerythroid forms of δ-aminolevulinate synthetase" @default.
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- W1967138751 doi "https://doi.org/10.1016/0003-9861(81)90105-3" @default.
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