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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Purification and substrate specificity of polymorphic forms of esterase D from human erythrocytes. Scott, E.M., Wright, R.C. Am. J. Hum. Genet. (1978) [Pubmed]
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