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Clinical Chemistry 39: 112-118, 1993;
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Clinical Chemistry, Vol 39, 112-118, Copyright © 1993 by American Association for Clinical Chemistry

Evaluation of silyl-blocked p-nitrophenylmaltoheptaoside as a substrate for alpha-amylase reagents

CS Elbin, S Becks and CA Lepp
Department of Research and Development, 810 S.D. Corporation, Westlake, OH 44145.

We describe a reagent for measuring alpha-amylase (EC 3.2.1.1) activity in serum with use of a thexyldimethylsilyl ether of p-nitrophenyl-alpha- D-maltoheptaoside (SB7) as substrate. This substrate differs from Genzyme's benzylidene-blocked p-nitrophenylmaltoheptaoside substrate (B- PNPG7). The reagent, optimized for the characteristics of the silyl- blocked substrate, contains 4-(2-hydroxyethyl)-1-piperazineethane sulfonate buffer at pH 7.3, alpha-glucosidase (maltase; EC 3.2.1.20), and glucoamylase (EC 3.2.1.3). Comparison with Ciba Corning Diagnostics Corp.'s, amylase reagent with B-PNPG7 as substrate (x) yielded a regression equation of y = 1.20x-2.7 (r = 0.9997). The linear range exceeded amylase concentrations > 2500 U/L and total precision (CV) was 2.3% at an amylase concentration of 112 U/L with the Ciba Corning 550 Express analyzer. Reconstituted reagent is stable for 30 days at 5 degrees C and 7 days at ambient (18-25 degrees C) temperatures.




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Copyright © 1993 by the American Association for Clinical Chemistry.