Die Beurteilung der exokrinen Pankreasfunktion mit Fluorescein-Dilaurat

Gregory, D. von; Opitz, H.

doi:10.1007/978-3-642-85453-8_247

Cited by 2 publications

(1 citation statement)

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“…The application of the oral pancreatic function test based upon FDL [12,[17][18][19][20][21] revealed clinical data showing specificities and sensitivities in ranges of 90% [22][23][24], even up to 100% in cases of total pancreatec tomy or cystic fibrosis [23,25], These diag nostic values underline experimental results reported earlier [18,19,26] that the hydro lyzing enzyme was obviously exclusively of pancreatic origin. The separation of the lipo lytic enzymes, which are secreted in the hu man pancreatic juice, and the registration of their activities developed on fatty acid esters of quite different chemical and physical properties now led to the identification of cholesterol esterase.…”

Section: Discussionsupporting

confidence: 71%

Lipolytic Enzymes of the Human Pancreas

Meyer-Bertenrath¹

1982

Enzyme

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Cholesterol erster hydrolase (cholesterol esterase, EC 3.1.1.13) does not only act on cholesterol esters, but also on esters of fluorescein. Diesters as well as monoesters of this dye show neither color nor fluorescence, so that these compounds may be used as chromogenic or fluorogenic substrates. Splitting off the ester bonds immediately causes the return of the original properties of the fluorescein. Its dilaurate was found to be a specific substrate of cholesterol esterase, allowing the measurement of activities of this enzyme down to ranges of 0.01 U/l by a fluorometric assay.

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