|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
9
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|
pubmed:dateCreated |
1989-6-8
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|
pubmed:abstractText |
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.
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pubmed:language |
ger
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pubmed:journal |
|
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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|
pubmed:issn |
0031-7144
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
43
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
637-9
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|
pubmed:dateRevised |
2007-1-29
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|
pubmed:meshHeading |
|
|
pubmed:year |
1988
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|
pubmed:articleTitle |
[The determination of neutral metalloendopeptidase (enkephalinase A) in biological material].
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|
pubmed:affiliation |
Institut für Wirkstofforschung, Akademie der Wissenschaften der DDR, Berlin-Friedrichsfelde.
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pubmed:publicationType |
Journal Article,
English Abstract
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