Purification and substrate specificity of polymorphic forms of esterase D from human erythrocytes.
Esterase D (EsD), purified from human erythrocytes and tested with a variety of substrates, hydrolyzed only triacetin, tributyrin, and certain soluble aryl esters of aliphatic acids. Esters of 4-methylumbelliferone were easily the best substrates. When the three genetically different isozymes were compared, the less common forms, EsD 2 and EsD 2-1, were less stable than EsD 1. With some substrates, the Michaelis constant of the EsD 2 form differed from that of the EsD 1 form. The EsD 2-1 hybrid form was usually, but not invariably, intermediate in properties. The physiologic significance of the genetic variability of this enzyme is unknown.
D004912:Erythrocytes / Q000201:enzymology*; D004950:Esterases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D006579:Heterozygote; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D010641:Phenotype; D011110:Polymorphism, Genetic; D013379:Substrate Specificity
D007527:Isoenzymes; D004950:Esterases