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Clinica Chimica Acta 324 (2002) 61–71 /locate/clinchim An enzymatic method for the measurement of glycated albumin in biological samples * Takuji Kouzuma , Tomomi Usami, Masaru Yamakoshi, Mamoru Takahashi, Shigeyuki Imamura Diagnostics RD Department, Fine Chemicals and Diagnostics Division, Health Care Company, Asahi Kasei Corporation. 632-1, Mifuku, Ohito-cho, Tagata-gun, Shizuoka-ken, 410-2321, Japan Received 8 April 2002; received in revised form 10 June 2002; accepted 10 June 2002 Abstract Background : In order to determine glycated albumin more easily and rapidly, we developed a new enzymatic method for glycated albumin in blood samples. Methods : The method involves use of albumin-specific proteinase, ketoamine oxidase and serum albumin assay reagent. In the assay, glycated albumin is hydrolyzed to glycated amino acids by proteinase digestion, and ketoamine oxidase oxidizes the glycated amino acids to produce hydrogen peroxide, which is quantitatively measured. Glycated albumin is calculated as the percentage of glycated albumin in total albumin. Results : The calibration curve for glycated albumin concentration was linear (r =0.999) between 0.0 and 50.0 g/l and that for albumin concentration was linear (r =0.999) p p between 0.0 and 60.0 g/l. The analytical recoveries of exogenous glycated albumin added to serum were 100–102.5%. The within-run and between-run CVs were 0.45–0.67% and 1.09–1.26%, respectively. This method was free