[The determination of neutral metalloendopeptidase (enkephalinase A) in biological material].
The simple determination of the Neutral Metalloendopeptidase (NEP, Enkephalinase A) with the known fluorogenic substrate Dansyl-D-Ala-Gly-(pNO2)Phe-Gly is disturbed by high concentrations of the Angiotensin-Converting-Enzyme (ACE). ACE hydrolyzes this substrate too but to a smaller degree. In some tissues and body fluids a further substrate hydrolysis takes place by any indefinite proteases. Finally the enzymatic hydrolysis of the NEP-substrate is inhibited by phosphate ions. A method is proposed for the elimination of this disturbances in the NEP-determination with a phosphate-free buffer using two comparison tests with Lisinopril and o-Phenanthroline. The resulting NEP-activity is calculated very simple thereafter.
Heder
G
G
Institut für Wirkstofforschung, Akademie der Wissenschaften der DDR, Berlin-Friedrichsfelde.
Böttger
A
A
Siems
W E
WE
Halatsch
W R
WR
Steinmann
C
C
D003619:Dansyl Compounds; D006868:Hydrolysis; D007202:Indicators and Reagents; D015260:Neprilysin / Q000032:analysis*; D009842:Oligopeptides; D007703:Peptidyl-Dipeptidase A / Q000032:analysis; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
D003619:Dansyl Compounds; D007202:Indicators and Reagents; D009842:Oligopeptides; C043503:dansyl-alanyl-glycyl-4-nitrophenylalanyl-glycine; D007703:Peptidyl-Dipeptidase A; D015260:Neprilysin
Zur Bestimmung von Neutraler Metalloendopeptidase (Enkephalinase A) in biologischem Material.