Evidence for the specificity of esterase and lipase by the use of three chromogenic substrates

Evidence for the specificity of esterase and lipase by the use of three chromogenic substrates

1949

REP.G2032

The esterolytic powers of kidney, liver, and pancreas of six species were studied with three chromogenic substrates prepared from ,a-naphthol and fatty acids (C2, C12, C16, C18). Kidney and liver (esterase) hydrolyzed the acetate and laurate. Pancreas (esterase and lipase) hydrolyzed all three substrates. At the concentrations used, eserine inhibited esterase and lipase, arsenilate and fluoride inhibited esterase, quinine inhibited lipase, and taurocholate accelerated lipase and slightly inhibited esterase activity. Evidence is provided for the existence of two distinct enzymes, esterase and lipase. Ideal substrates for the former contain short chain fatty acids, and for the latter long chain fatty acids.

v.181:343-355, JOURNAL OF BIOLOGICAL CHEMISTRY

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