Discrepancies in measurement of aspartate aminotransferase by continuous-flow analysis.

1983 ◽  
Vol 29 (12) ◽  
pp. 2086-2088
Author(s):  
P West

Abstract I compared results for aspartate aminotransferase (EC 2.6.1.1) obtained with a reaction-rate analyzer (LKB 2086 Mark Two), based on IFCC methodology, and a continuous-flow analyzer (the Technicon SMA 2) for 115 patients' sera and seven commercial quality-control sera. The data from the SMA 2 showed a clear positive bias in those sera with activities exceeding 40 U/L (the upper limit of the reference range). Independent data to support the bias of the SMA 2 and other continuous-flow analyzer systems are presented. Application of a correction factor to the SMA 2 data above the upper limit of the range significantly decreased this bias. Failure to apply such a factor to data obtained from continuous-flow analyzers could lead to serious clinical misinterpretation.

1984 ◽  
Vol 30 (1) ◽  
pp. 129-131 ◽  
Author(s):  
R J Elin ◽  
B A Gray

Abstract Using a Technicon SMAC continuous-flow instrument, we compared a liquid quality-control material ("Decision level 3," Beckman) with two different lyophilized quality-control materials. The variances for 19 analytes in the three materials were significantly greater for Decision than for the Ortho Abnormal and the Omega II lyophilized control sera (p less than 0.00001 for each comparison by the omnibus test). The imprecision for Decision was not due to incomplete mixing or carryover. The viscosity of Decision, however, was more than twice that of the two lyophilized control sera or of pooled human serum.


1967 ◽  
Vol 13 (10) ◽  
pp. 847-854 ◽  
Author(s):  
Harold H Brown ◽  
Mary R Ebner

Abstract A simple technic to adapt the advantages of continuous flow analysis to the kinetic assay of multiple enzyme samples is described. It will permit adequate standardization by primary or secondary standards run through the entire analysis of those procedures that do not exhibit spontaneous changes in light absorption or fluorescence with time. The adaptation of the Kind-King method for alkaline phosphatase (1) to this technic is given to demonstrate the superiority of such a system over single-point enzyme assays.


1969 ◽  
Vol 15 (11) ◽  
pp. 1045-1055 ◽  
Author(s):  
R L Habig ◽  
B W Schlein ◽  
L Walters ◽  
R E Thiers

Abstract A system is described which permits measurements, such as photometry, to be made on air-segmented streams, as in continuous-flow analysis. Elimination of the "debubbler" step before measurement provides two basic assets: (1) more rapid attainment of steady-state conditions (lower interaction between samples), and (2) maintenance of the integrity of the bubbled analysis stream, permitting subsequent handling and remeasurement. A device has been developed for detecting air bubbles. When placed across the light path of a photometer flow cell it inactivates the readout system when bubbles pass by. The resulting system measures the transmittance of each individual liquid segment of the analysis stream, while maintaining the integrity of the stream. Two examples of possible applications of this system are described. One is a simple total-protein determination with biuret, at three times the conventional sampling rate. The other is a continuous-flow, two-point, reaction-rate method for assay of alkaline phosphatase activity.


1981 ◽  
Vol 123 ◽  
pp. 239-246 ◽  
Author(s):  
Herbert Weisz ◽  
Günter Fritz

2020 ◽  
Vol 155 ◽  
pp. 104731 ◽  
Author(s):  
Marcos Almeida Bezerra ◽  
Valfredo Azevedo Lemos ◽  
Djalma Menezes de Oliveira ◽  
Cleber Galvão Novaes ◽  
Jeferson Alves Barreto ◽  
...  

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