Fractionation and further characterization of granulocytic and monocytic alpha-naphthyl acetate (ANAE) esterases.
Following characterization of myeloid nonspecific esterases by isoelectric focusing (IEF), two main groups of alpha-naphthyl acetate (ANAE) esterase isoenzymes were defined and fractionated from cytoplasmic extracts by chromato focusing techniques according to differences in their isoelectric points (pI). The first of these ANAE enzyme groups was common to leukocytes of both granulocytic and monocytic lineage, while the other, which characteristically comprised a group of isoenzymes within the pI range 5.5-6.1, was specifically associated with monocytic differentiation. The properties of the two purified ANAE enzyme fractions were compared by inhibition (heat and sodium fluoride) and further electrophoretic studies, and the results discussed in relation to the cytochemical characterization of these enzymes as markers of specific myeloid cell differentiation.
D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification*; D004586:Electrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D006098:Granulocytes / Q000201:enzymology*; D006358:Hot Temperature; D006801:Humans; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification*; D007938:Leukemia / Q000201:enzymology; D009000:Monocytes / Q000201:enzymology*; D009283:Naphthol AS D Esterase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D012969:Sodium Fluoride / Q000494:pharmacology
D007527:Isoenzymes; D012969:Sodium Fluoride; D009283:Naphthol AS D Esterase; D002265:Carboxylic Ester Hydrolases