Studies on blood esterases : purification and characterization of a butyrylesterase from human erythrocytes

• The object of these studies has been blood esterasesi and especially a butyrylesterase present in human erythrocytes. First, thiophenyl esters were synthesized for use as substrates in assaying arylesterases according to the ElIman procedure. These substrates were found to be appropriate for investigating arylesterase I in bovine plasma and arylesterase I and II in porcine plasma. Human erythrocytes were also found to contain a high molecular weight, eserine-insensitive esterase capable of hydrolysing butyryl esters. Judging from ease of release of this enzyme from the red blood cells upon lysis, the butyrylesterase is cytoplasmic. This enzyme was purified using ion-exchange chromatography, gel filtration, and chromatography on hydroxyapatite and characterized in terms of substrate specificity, inhibitor patterns molecular weight, isoelectric point, and amino acid composition. On the basis of these studies, the erythrocyte butyrylesterase was concluded to be a serine hydrolase containing a cysteine residue(s) essential for its catalytic activity. 

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NATURVETENSKAP  -- Biologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

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