Appeal No. 1996-1960
Application No. 07/975,167
OPINION
Kasahara describes methods and reagents for measuring lipase activity characterized by using a
water-soluble glyco-fatty acid ester substrate, wherein the fatty acid ester residue has about 5-22
carbon atoms and is bonded on the hydroxy groups of a mono-, oligo- or poly-saccharide, e.g.,
glucose, maltose or starch (page 3, lines 17-30; page 4, lines 1-2 and 9-11), e.g., at the hydroxyl
group(s) at the 1- and/or 6-position of the saccharide terminal (page 4, lines 9-15). Examples include
6-O-palmitoyl glucose (page 4, lines 17-18) and 6-O-oleyl maltose (page 6, line 23). Lipase cleaves
the substrate into its constituent saccharide and fatty acid (page 4, lines 20-22) and either the amount of
the saccharide or fatty acid formed is determined as a measurement of lipase activity (page 4, lines 29-
30). For example, if the saccharide is maltose, the amount of maltose formed by the lipase reaction
may be quantitated by reacting the maltose with maltase (i.e., "-glucosidase) to form glucose, which
glucose is then oxidized by glucose oxidase to produce hydrogen peroxide which is then measured
colorimetrically by a 4-aminoantipyrine-phenol-peroxidase reaction (page 5, lines 1-6; page 9,
penultimate line and pages 8-9, Application Example 2).
McCroskey describes temperature-independent methods and reagents for determining the
activity of enzymes which can hydrolyze substrates capable of releasing p-nitrophenol (col. 1, lines 31-
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