�ber die Aminopeptidaseaktivit�t des Schwangerenserums und ihre Beziehung zu dessen Verm�gen, Oxytocin zu inaktivieren

Fractionation and characterization of cystine aminopeptidase (oxytocinase) and arylamidase of the human placenta

“…Beside the natural substrates, this enzyme also hydrolyses several synthetic substrates, e.g. L-cystine-di-ß-naphthylamide and L-leucine-ß-naphthylamide (Tuppy & Nesvadba, 1957), L-cystine-bis-p-nitroanilide (Tovey, 1969) and Sbenzyl-L-cysteine-p-nitroanilide (Small & Watkins, 1974). It is possible that none of these substrates can be regarded specific for oxytocinase, and part of the hydrolysis may be caused by other aminopeptidases.…”

Contributions of Histochemistry to the Development of the Proteolytic Enzyme Detection System in Diagnostic Medicine

“…In delving back through the literature, to the best of my findings, Green and co-workers were the first to employ the Bratton-Marshall method with a /3-naphthylamide substrate for identifying a protease in human serum, and to further demonstrate that leucine aminopeptidase was elevated in sera from pregnant women. In 1957 Tuppy and Nesvadba (67) reported several new substrates that were employed in the study of serum aminopeptidases in pregnant women; among the compounds were L-cystine di-/3-naphthylamide and D,imethionine /3-naphthylamide. In 1958 Rosenblatt et al (53) reported the synthesis of L-leucyl-4-methoxy-/3-naphthylamide; Nachlas et al (41) subsequently reported (in 1960) on the histochemical application of the modified leucyl substrate, and claimed that the presence of the methoxy group in the 4 position permitted coupling 40 times as fast as 2-naphthylamine.…”

Human chorionic somatomammotropin, estriol and oxytocinase as indexes of fetal growth

“…The variance analysis did not show statistical differences between these diseases. Oxytocinase activity was determined by a colorimetric method, using L-cystine-di-B-naftilamide äs Substrate [29]. All newborns were weighed using the same scale and during the first hour of life.…”