Abstract: A spectrophotometric assay for the detection of acetaminophen in aqueous fluids can be carried out with a dry analytical element. The element comprises a support having thereon one or more reagent layers containing a first enzyme, aryl acylamidase, to cleave the amide bond of acetaminophen to produce p-aminophenol; a second enzyme, ascorbic acid oxidase, to oxidize the p-aminophenol so that it couples to a water soluble coupling agent to form a dye that is read at 670 nm. The assay is precise, accurate on serum and plasma samples, and relatively free from significant interferences. The element also allows measurement over a broad dynamic range.

Abstract: A chromatographic material comprising an inorganic support-polysaccharide particle matrix is described. The matrix comprises an inorganic support having a high surface density of hydroxyl groups and, covalently attached thereto, insoluble particles of a polysaccharide. The free hydroxyl groups of the matrix can be activated, say, by treatment with cyanogen bromide or sodium metaperiodate, to form active sites where ligands can be attached for affinity chromatography.

Abstract: Catalase is effectively removed from a uricase preparation by amphiphilic chromotography using as the column material cyanogen bromide-activated polysaccharide having a hydrophobic ligand attached thereto. Particularly useful hydrophobic ligands are the alkanediamines.

Abstract: Cholesterol esterase is purified by removal of the separable lipase in an enzyme preparation containing both cholesterol esterase and lipase activities by treatment using a hydrophobic chromatography column comprising carboxylated polysaccharide material having lower alkylamine with less than 8 carbon atoms attached thereto.