The use of immobilized uricase/ aldehyde dehydrogenase nylon-tube reactors in the automated determination of uric acid in serum

1980 ◽  
Vol 301 (2) ◽  
pp. 161-161 ◽  
Author(s):  
W. Hinsch ◽  
A. Antonijevic ◽  
P. V. Sundaram
1974 ◽  
Vol 137 (1) ◽  
pp. 25-32 ◽  
Author(s):  
D. J. Inman ◽  
W. E. Hornby

1. Glucose oxidase (EC 1.1.3.4), amyloglucosidase (EC 3.2.1.3), invertase (EC 3.2.1.26) and β-galactosidase (EC 3.2.1.23) were covalently attached via glutaraldehyde to the inside surface of nylon tube. 2. The linked enzyme system, comprising invertase immobilized within a nylon tube acting in series with glucose oxidase immobilized in a similar way, was used for the automated determination of sucrose. 3. The linked enzyme system, comprising β-galactosidase immobilized within a nylon tube acting in series with glucose oxidase immobilized in a similar way, was used for the automated determination of lactose. 4. The linked enzyme system, comprising amyloglucosidase immobilized within a nylon tube acting in series with glucose oxidase immobilized in a similar way, was used for the automated determination of maltose. 5. Mixtures of glucose oxidase and amyloglucosidase were immobilized within the same piece of nylon tube and used for the automated determination of maltose. 6. Mixtures of glucose oxidase and invertase were immobilized within the same piece of nylon tube and used for the automated determination of sucrose.


1979 ◽  
Vol 25 (4) ◽  
pp. 619-621 ◽  
Author(s):  
K Bartl ◽  
M Brandhuber ◽  
J Ziegenhorn

Abstract The enzymatic determination of serum uric acid by use of uricase, catalase, and aldehyde dehydrogenase according to Haeckel [J. Clin. Chem. Clin Biochem. 14, 101 (1976)] showed interferences from ethanol-converting enzymes, which are present in some patients' sera. We have identified these enzymes as alcohol dehydrogenase isoenzymes. Among other substances, a mixture of pyrazole and oxalate can be used to eliminate these interferences. This inhibitor system gives good results when used in the automated kinetic uric acid determination, as is shown by a comparison with the manual assay for uric acid according to Kageyama [Clin. Chim. Acta 31, 421 (1971)].


1977 ◽  
Vol 23 (9) ◽  
pp. 1538-1540 ◽  
Author(s):  
R M White ◽  
R E Cross ◽  
J Savory

Abstract An early-reading blank-corrected end-point determination of uric acid in serum has been developed for use with a centrifugal analyzer. The method is based on a modification of the uricase (urate:oxygen oxidoreductase, EC 1.7.3.3)/catalase (hydrogen peroxide:hydrogen peroxide oxidoreductase EC 1.11.1.6)/aldehyde dehydrogenase (aldehyde:NAD(P)+ oxidoreductase, EC 1.2.1.5)-coupled analytical scheme reported by Haeckel [Z. Klin. Chem. Klin. Biochem. 14, 101 (1976)]. Sensitivity and precision of the method are excellent, and results compare well with those obtained by the Kageyama procedure [Clin. Chim. Acta 31, 421 (1971)].


1966 ◽  
Vol 12 (11) ◽  
pp. 748-766 ◽  
Author(s):  
Stanley Morgenstern ◽  
Richard V Flor ◽  
James H Kaufman ◽  
Bernard Klein

Abstract An automated procedure is presented for the enzymatic determination of serum uric acid on both the AutoAnalyzer and the Robot Chemist. The procedure measures as the neocuproine complex, the difference in the amount of Cu+ formed by reaction of a Cu++-alkanolamine buffered solution with serum uric acid under precisely controlled conditions before and after uricase treatment of the serum. The difference is proportional to the true serum uric acid content. The elements contributing to the enzymatic reaction, the colorimetric reaction, and the elimination of interferences were investigated. Comparison of serum uric acid values obtained by this method with those obtained by ultraviolet spectrophotometry show very good agreement.


1980 ◽  
Vol 26 (12) ◽  
pp. 1652-1655 ◽  
Author(s):  
W Hinsch ◽  
A Antonijewić ◽  
P V Sundaram

Abstract We describe routine methods for determining glucose in plasma with use of aldehyde dehydrogenase or glucose oxidase-aldehyde dehydrogenase immobilized in a nylon tube that is integrated into a continuous-flow system. Although the coupled-enzyme nylon-tube reactors require the presence of a third enzyme, catalase, in solution, the kinetics are not so complicated as to preclude reliable routine determination of glucose at very low cost. Precision is good, and results correlate well with those by the method involving glucose oxidase in solution. More than 3000 tests may be carried out with one reactor. The immobilized enzymes are stable for several months at 4 degrees C when not in use.


1975 ◽  
Vol 147 (3) ◽  
pp. 593-603 ◽  
Author(s):  
D L Morris ◽  
J Campbell ◽  
W E Hornby

Triethyloxonium tetrafluoroborate was used to O-alkylate nylon-tube thus producing the imidate salt of the nylon which was further made to react with 1,6-diaminohexane. 2. Hexokinase (EC 2.7.1.1) and glucose 6-phosphate dehydrogenase (EC 1.1.1.49) were immobilized on the amino-substituted nylon tube through glutaraldeyde and bisimidates. 3. The effect of varying the conditions of O-alkylation and the amount of enzyme immobilized on the activity of nylon tube-hexokinase derivatives was determined. 4. The effect of varying the amount of enzyme immobilized on the activity of nylon-tube-glucose 6-phosphate dehydrogenase derivatives was determined. 5. The thermal stability of nylon-tube-hexokinase and nylon-tube-glucose 6-phosphate dehydrogenase derivatives was studied. 6. Different ratios of hexokinase and glucose 6-phosphate dehydrogenase were co-immobilized on nylon tube, and the rate of conversion of glucose into 6-phosphogluconolactone was compared with the individual activities of the immobilized enzymes. 7. Hexokinase and glucose 6-phosphate dehydrogenase co-immobilized on nylon tube were used in the automated analysis of glucose.


1971 ◽  
Vol 17 (12) ◽  
pp. 1154-1159 ◽  
Author(s):  
Nathan Gochman ◽  
Joan M Schmitz

Abstract An automated colorimetric procedure is described for the determination of serum and urine uric acid with improved specificity. Hydrogen peroxide, formed when uric acid is oxidized by uricase, oxidatively couples with 3-methyl-2-benzothiazolinone hydrazone and N,N-dimethylaniline, in the presence of peroxidase, to produce a stable, sensitive indamine dye. The method is reproducible, and the results correlate well with those obtained by a manual spectrophotometric uricase procedure. Also, the automated procedure is resistant to many added reducing substances that cause positive interferences in alkaline phosphotungstate methods.


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