Amidase Activity of Urokinase I. Hydrolysis of a-N-Acetyl-L-Lysine p-Nitroanilide

Autor:	M Karadjova, E Christova, D Petkov
Rok vydání:	1973
Předmět:	Urokinase Hydrolysis Stereochemistry Chemistry Lysine medicine Amidase activity Alpha (ethology) Hematology medicine.drug
Zdroj:	Thrombosis and Haemostasis. 29:276-285
ISSN:	2567-689X 0340-6245
DOI:	10.1055/s-0038-1647770
Popis:	Summaryα-N-acetyl-L-lysine p-nitroanilide (ALNA) was synthesized as a low-molecular weight model of the natural urokinase substrate plasminogen. Urokinase was found to catalyse anilide bond cleavage. The extent of hydrolysis can be followed spectro- photometrically by using the strong absorption band of one of the products p-nitro- aniline. An accurate, continuous and convenient assay for urokinase is proposed. As determined by the kinetic study, Vmax5 a measure for the sensitivity of an assay, is about 8 times higher than that obtained for the most sensitive urokinase ester substrates. This was demonstrated by its use for tracing the elution of urokinase during the purification of the enzyme by column chromatography.The high apparant Km value obtained is discussed in terms of the mechanism of serine proteinase action on esters and amides.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::e4d2dbd764ffb5d2c5f28b8f88e516d9 https://doi.org/10.1055/s-0038-1647770 Zobrazit plný text záznamu