Artigo Revisado por pares

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

ISSN

1878-1454

Autores

Yvonne Piquilloud, A. Reinharz, Marc Roth,

Tópico(s)

Electrochemical sensors and biosensors

Resumo

A 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 ZPheHisLeu and ZProPheHisLeu are hydrolysed by the equine and human enzymes. ZPheHisLeu is hydrolysed about 10 times faster than angiotensin I and ZProPheHisLeu 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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