Studies on the angiotensin converting enzyme with different substrates
1970; Elsevier BV; Volume: 206; Issue: 1 Linguagem: Inglês
10.1016/0005-2744(70)90090-2
ISSN1878-1454
AutoresYvonne Piquilloud, A. Reinharz, Marc Roth,
Tópico(s)Electrochemical sensors and biosensors
ResumoA method has been developed for the chemical assay of the angiotensin converting enzyme. It is based on the fluorimetric determination of histidyl-leucine, a product of the enzymic reaction. It is shown that not only angiotensin I, but also the artificial substrates ZPheHisLeu and ZProPheHisLeu are hydrolysed by the equine and human enzymes. ZPheHisLeu is hydrolysed about 10 times faster than angiotensin I and ZProPheHisLeu by the humanenzyme, and is therefore a convenient substrate for quantitative determinations. Investigations in which this new substrate was utilized showed that human converting enzyme inactivated by dialysis was reactivated by anions in the order Cl− > NO3− > Br− > F− > I−. The enzyme activity is highest between pH 7.5 and 8.5.
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