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Clinical Chemistry, Vol 21, 1479-1485, Copyright © 1975 by the American Association for Clinical Chemistry
1 Department of Diagnostic Research, Hoffmann-La Roche Inc.,
Nutley, N.J. 07110.
The elements of the mechanized fluorometric lipase (EC 3.1.1.3) assay of Fleisher and Schwartz [Clin. Chem. 17, 417 (1971)] were made optimum; a manual adaptation was also developed. Hydrolysis of the monodecanoyl fluorescein substrate by hog pancreatic lipase is a zero-order reaction. The hydrolytic activity of normal human serum, serum from hospitalized patients without pancreatitis, and serum from patients with acute pancreatitis showed considerable overlap. Bile salts, considered activators in titrimetric or turbidimetric lipase assays, inhibited hydrolysis of the substrate by human serum. We conclude that monodecanoyl fluorescein is not a specific substrate for the serum lipase measured in acute pancreatitis.
Submitted on May 21, 1975
Accepted on June 19, 1975
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