PMID: 10611Aug 25, 1976

Studies on the pH-dependence, inhibition and reactivation of angiotension II-amide splitting enzymes in human erythrocytes (author's transl)

Research in Experimental Medicine. Zeitschrift Für Die Gesamte Experimentelle Medizin Einschliesslich Experimenteller Chirurgie
H P NastH P Wolff


Aminopeptidase activity of three fractions of human erythrocytes (membranes free of hemoglobin; hemolysate free of membranes; enzyme protein fraction made free of hemoglobin by DEAE-cellulose) was measured by a NADH dependent optical test using asparaginyl1-angiotension II-amide as substrate. 1. From the enzyme protein fraction 6 subfractions were obtained by (NH4)2SO4 precipitation. By measuring enzyme kinetics at three different pH-values (pH 5,0; 7,0; 8,0) with and without addition of the effectors Na2EDTA and Ca++ the existence of 6 different enzymes could be demonstrated. 2. The aminopeptidase activity of the hemolysate made free of membranes could be inhibited by diisopropylfluorphosphate and p-chloromercuribenzoate at three different pH-values (pH 5,0; 6,5; 7,0; 8,0 and 6,5; 7,0; 8,0 respectively). 3. A reduction of enzymatic activity of 20% was found after incubation at 37degreesC for two hours.


Jan 1, 1966·Clinica Chimica Acta; International Journal of Clinical Chemistry·T KokubuY Yamamura
Nov 1, 1967·The American Journal of the Medical Sciences·H D Itskovitz, L Miller
Jan 1, 1969·Pflügers Archiv : European journal of physiology·H DahlheimK Thurau
Dec 15, 1970·Experientia·M Matsunaga, G M Masson
Apr 1, 1961·Physiological Reviews·I H PAGE, F M BUMPUS
Jun 1, 1962·The Journal of Clinical Investigation·M A HENNESSEYB W GABRIO
May 1, 1963·The Journal of Clinical Investigation·R B HICKLERG W THORN
Feb 1, 1963·Archives of Biochemistry and Biophysics·F J BEHALE C KELLY
Apr 15, 1963·Klinische Wochenschrift·D KLAUSH PFEIL
Oct 1, 1964·Metabolism: Clinical and Experimental·B RINIKER

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