Continuous-flow potentiometric determination of α-amylase activity in serum and urine

1985 ◽  
Vol 32 (2) ◽  
pp. 183-190
Author(s):  
E.P. Diamandis ◽  
A. Papanastasiou-Diamandi ◽  
T.K. Christopoulos ◽  
T.P. Hadjiioannou
1975 ◽  
Vol 21 (6) ◽  
pp. 694-702 ◽  
Author(s):  
Henning F Proelss ◽  
Billy W Wright

Abstract We report a new method for the mechanized determination of serum and urinary alpha-amylase by use of a continuous-flow system, based on the measurement of maltose formed by incubating the sample with amylodextrin at pH 7 and 40 °C. After dialysis, maltose is converted enzymatically to glucose, which is measured by Trinder's glucose oxidase—peroxidase method [J. Clin. Pathol. 22, 246 (1969)]. The reaction is linear for amylase activities up to 1400 Somogyi units/dl (2560 U/liter) and for maltose concentrations through 1500 mg/dl. No blank assay is required; consequently precision is improved and the automated system is simplified. Calibration with primary maltose standards increases accuracy and reliability. Common reducing substances in serum and urine do not interfere at their normal concentrations. There is a linear correlation between the results of this method and those of chromogenic and iodometric methods for normal and pathologic sera and urines. The chromogenic method yields significantly higher results and the iodometric method significantly lower results than this maltogenic method for elevated amylase activities. The normal range is 40-140 Somogyi units/dl (73-256 U/liter).


1991 ◽  
Vol 37 (8) ◽  
pp. 1323-1328
Author(s):  
Z Ogawa ◽  
Y Matsubayashi ◽  
S Satoh ◽  
N Orita ◽  
H Itoh

Abstract We synthesized o-(4,6-o-isopropylidene-alpha-D-glucopyranosyl)-(1----4)- [o-alpha-D-glucopyranosyl-(1----4])5-o-alpha-D-glucopyranosyl-(1----2)- alpha-D-fructofuranoside (IPG7F) and developed an assay for determining the activity of amylase in human serum and urine by using this substrate. Glucoamylase, alpha-glucosidase, and mannitol dehydrogenase are used as coupling enzymes. The coupled reactions are monitored by continuously measuring the oxidation rate of NADH. In this procedure, various substances in the test specimens do not interfere with the detection of amylase activity. Exactly one molecule of NADH is oxidized by one attack of amylase on the substrate, although four products can be produced in the reaction. The within-assay coefficient of variation (CV) ranged from 1.0% to 4.1% and the between-assay CV ranged from 2.6% to 5.3%. The results of our new assay correlate well with those of the amylase assay involving p-nitrophenol maltoheptaoside as substrate (r = 0.978) and with those of the amylase assay involving maltopentaose (r = 0.987).


1979 ◽  
Vol 25 (3) ◽  
pp. 481-483 ◽  
Author(s):  
K J Whitlow ◽  
N Gochman ◽  
R L Forrester ◽  
L J Wataji

Abstract The use of maltotetraose ss a new substrate for the enzyme-coupled determination of amylase activity in biological fluids was developed by Beckman Microbics. We evaluated a manual and a centrifugal analyzer version of the method in comparison with two commonly used manual starch-dye amylase techniques: Roche Amylochrome and Pharmacia Phadebas. Both maltotetraose amylase procedures proved to be rapid and precise, and results correlated satisfactorily with the starch-dye methods for serum and urine samples.


1978 ◽  
Vol 24 (5) ◽  
pp. 747-750 ◽  
Author(s):  
S J Soldin ◽  
J G Hill

Abstract We describe a procedure for the rapid and specific measurement of creatinine, in which it is separated from other compounds in serum or urine by paired-ion chromatography and is quantified by measuring its absorbance at 200 nm. The procedure can be done on as little as 10 microliter of serum. Between-day precision studies for concentrations of 13 and 62 mg/liter yielded coefficients of variation of 6.9 and 2.2%, respectively. Analytical recovery of various amounts of creatinine added to plasma exceeded 95% in all cases. The proposed procedure was compared with the continuous-flow procedure by analyzing a series of serum and urine specimens by both methods. There was excellent agreement for urine specimens, but with serum the results by the present method were significantly (P less than 0.001) lower.


The Analyst ◽  
2015 ◽  
Vol 140 (4) ◽  
pp. 1161-1165 ◽  
Author(s):  
Qing Wang ◽  
Hui Wang ◽  
Xiaohai Yang ◽  
Kemin Wang ◽  
Rongjuan Liu ◽  
...  

A one-step assay for direct determination of α-amylase activity in serum and urine was developed using a portable personal glucose meter.


1972 ◽  
Vol 42 (1) ◽  
pp. 63-66 ◽  
Author(s):  
Irie Akiko ◽  
Hunaki Masaaki ◽  
Bando Keiichi ◽  
Kawai Kazuo

Author(s):  
W. G. Brydon

The fluorometric method of Fingerhut et al. (1969) for the determination of serum calcium has been modified to approximately treble the sensitivity. Using only 120 μl of sample a method has been developed for the simultaneous determination of calcium and inorganic phosphate in serum and urine, the phosphate being measured by complexing phosphomolybdate with methyl green, a method developed by Van Belle (1970). Only a single dialysis stage is required, and reagents and sample can be delivered using an AutoAnalyzer Pump I. The techniques correlate well with other methods. Accuracy and precision data are presented.


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