Pteroylpolyglutamate hydrolase of human granulocytes. I. Partial purification and kinetic studies.
Pteroylpolyglutamate hydrolase was demonstrated in the lysosome-like cytoplasmic granules of human granulocytes. Partial purification of this enzyme from granulocytes, obtained from patients with chronic myeloid leukaemia, was achieved by chromatography of the granule extract on Sephadex G-75, Bio-Rex 70 and hydroxylapatite. The enzyme preparation obtained was slightly contaminated with myeloperoxidase. Synthetic pteroyltetraglutamate was used as a substrate for the enzyme. The pH optimum was 5.1; the Km was 6 x 10(-3) mol/l; and the enzyme was activated by divalent cations, e.g. Ca++, Mg++ and Mn++. Pteroylpolyglutamate hydrolase is suggested to be involved in the destruction of microorganisms in granulocytes during phagocytosis.
D001681:Biological Assay; D002268:Carboxypeptidases / Q000302:isolation & purification*; D002845:Chromatography; D002850:Chromatography, Gel; D004789:Enzyme Activation; D006098:Granulocytes / Q000032:analysis / Q000201:enzymology*; D006801:Humans; D006882:Hydroxyapatites; D007700:Kinetics; D010587:Phagocytosis; D011623:gamma-Glutamyl Hydrolase / Q000097:blood / Q000302:isolation & purification*
D006882:Hydroxyapatites; D002268:Carboxypeptidases; D011623:gamma-Glutamyl Hydrolase