EVALUATION OF SILYL-BLOCKED P-NITROPHENYLMALTOHEPTAOSIDE AS A SUBSTRATE FOR ALPHA-AMYLASE REAGENTS

被引：0

作者：

ELBIN, CS

BECKS, S

LEPP, CA

机构：

[1] CIBA CORNING DIAGNOST CORP,DEPT SYST ENGN,OBERLIN,OH 44074

[2] OLYMPUS CORP,DIV CLIN INSTRUMENTS,LAKE SUCCESS,NY 11042

来源：

CLINICAL CHEMISTRY | 1993年 / 39卷 / 01期

关键词：

ENZYME ACTIVITY; SYNTHETIC SUBSTRATES; BICHROMATIC ANALYSIS;

D O I：

暂无

中图分类号：

R446 [实验室诊断]; R-33 [实验医学、医学实验];

学科分类号：

1001 ;

摘要：

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 Coming 550 Express(R) analyzer. Reconstituted reagent is stable for 30 days at 5-degrees-C and 7 days at ambient (18-25-degrees-C) temperatures.

引用

页码：112 / 118

页数：7