[Determination of the catalytic activity of lipase with trilinolein as substrate].
The applicability of the two point test reported by Proelss & Wright ((1977) Clin. Chem. 23, 522-531) for the determination of lipase was investigated. The substrate, trilinolein, is indeed cleaved by pancreatic lipase without interference from liver esterase or cholinesterase; on the other hand, the reported colour reaction gives nonreproducible results. Furthermore, the continuous UV-test showed a lag phase, the duration of which depends on the added catalytic activity. For these reasons the method of Proelss & Wright for the determination of lipase in serum does not give diagnostically useful results.
D001647:Bile Acids and Salts / Q000378:metabolism; D002384:Catalysis; D006801:Humans; D008041:Linoleic Acids / Q000378:metabolism; D008049:Lipase / Q000032:analysis*; D008084:Lipoxygenase / Q000378:metabolism; D010783:Photometry / Q000379:methods; D013379:Substrate Specificity; D014280:Triglycerides / Q000378:metabolism*
D001647:Bile Acids and Salts; D008041:Linoleic Acids; D014280:Triglycerides; D008084:Lipoxygenase; D008049:Lipase; C009564:trilinolein
Zur Bestimmung der katalytischen Aktivität der Lipase mit Trilinolein als Substrat.