作者: DARRELL DOYLE , ROBERT MITCHELL
DOI: 10.1016/B978-0-12-472703-8.50060-3
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摘要: ABSTRACT. δ-Aminolevulinate dehydratase isolated from fetal liver and a hepatoma has been compared to the enzyme adult liver. The is less stable denaturation by heat catalytically more efficient than fast growing same properties as enzymes all three tissue sources are similar in molecular size, electrophoretic mobility, apparent K m for substrate, δ-aminolevulinic acid, number of active sites, pattern peptides released trypsin. These results indicate that cellular mechanism controlling structure δ-aminolevulinate expressed again combined genetic-biochemical approach can provide insight into this regulation.