L. Svendsen
2017
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Abstract
wherein R1 is alkanoyl or co-aminoalkyanoyl, phenylal kanoyl or p-aminophenylalkanoyl, cyclohexylcarbonyl or 4-aminomethyl-cylcohexylcarbonyl, benzoyl option ally substituted with methyl, amino, or halogen in the o or p-position, alkoxy carbonyl, benzyloxy carbonyl optionally substituted with methoxy, methyl, or chlo rine in the p-position, alkylsulfonyl, phenylsulfonyl or naphthylsulfonyl, R2 is straight-chained or branched alkyl, hydroxyalkyl, alkoxyalkyl, benzoxyalkyl, oy-car boxy-alkyl, c)-alkoxy carbonylalkyl, c)-benzyloxycarbo nylalkyl, cyclohexyl, cyclohexylmethyl, 4-hydroxycy clohexylmethyl, phenyl, benzyl, 4-hydroxybenzyl or imidazol-4-yl-methyl, R3 is hydrogen or alkyl, R is hydrogen, methyl or ethyl, and R5 is an amino group substituted with aromatic or heterocyclic radicals, R. being capable of being split off by enzymatic hydrolysis to form a colored or fluorescent product H-Rs. The tripeptide derivatives of formula I are used for assaying certain enzymes, and in particular, factor Xa. Enzyme bearing materials are reacted with the said tripeptide derivatives. The quantity of split product H-R5 released by the enzymatic action on the tripeptide derivative is determined photometrically, spectrophotometrically, fluorescence-spectrophotometrically, or electrochemi cally. The quantity of released split product H-R per time unit is proportional to the quantity of enzyme pres ent in the starting material.