scholarly journals Automation of the Turbidimetric Determination of Serum Lipase

Author(s):  
M. Puukka ◽  
Raija Puukka

A turbidimetric procedure for the determination of serum lipase activity has been adapted for use on a System Olli 3000 analyser. In this automated procedure 50 μl of serum and standard sample, and a buffer solution, are pipetted into disposable cuvettes in the measurement block. The block is then preincubated for 15 minutes at 37°C, and after simultaneous addition of the olive oil emulsion, the absorbances of the cuvettes are recorded simultaneously for two minutes at 405 nm. Using the program ‘block standards’ for the calibration of the method the results are ready in graphic form and expressed as U/l within about five minutes of the addition of the olive oil. A total of 60 patient sera can be analysed in half an hour. The method is linear up to at least 1000 U/l, and the reference values are between 11 and 140 U/l. A comparison of the method with the modification of the Cherry-Crandall titrimetric method gives a value of 0·87 for the correlation coefficient and the regression equation y = 0·97x + 12 (n = 191). Within-run precision (CV) for sera with mean enzyme activities of 149 and 354 U/l was found to be 4·2% and 3·4%, respectively (n = 20), and day-to-day precision 5·0% (mean activity = 339 U/l, n = 18).

1971 ◽  
Vol 17 (12) ◽  
pp. 1150-1153 ◽  
Author(s):  
Zakariya K Shihabi ◽  
Charles Bishop

Abstract Serum lipase is determined by following turbidity changes during two 1-min intervals after adding serum to an olive oil emulsion containing desoxycholate. The olive oil emulsion is simply prepared and is stable for a month under refrigeration. Our observations confirm the findings of other investigators that increases in serum lipase activity are more accentuated than increases in serum amylase activity during pancreatitis. With the present fast and convenient method, serum lipase appears to be a better test for pancreatitis than is serum amylase.


2014 ◽  
Vol 3 (4) ◽  
pp. 119 ◽  
Author(s):  
Raffaele Romano ◽  
Nadia Manzo ◽  
Immacolata Montefusco ◽  
Annalisa Romano ◽  
Antonello Santini

<p>In this study the use of liquid carbon dioxide, CO<sub>2</sub>, for extraction of oil from olive paste (<em>Peranzana cultivar</em>)<strong> </strong>were examined and extracted oil was compared with oils obtained by centrifugation, pressure and use of chemical solvent.</p> <p>It is well known that the use of CO<sub>2</sub> has many advantages: miscibility with a wide range of molecules, food safety, non-flammability, absence of residues in the extract, possibility of total solvent recovery and no production of olive mill waste water that are highly polluting for the environment and require expansive disposal.</p> <p>Samples were subjected to the following analyses: determination of Free Fatty Acids (FFA), Peroxides Value (PV), Spectrophotometric Indices, Fatty Acids Composition (FA), determination of biophenols content and determination of Volatile Organic Compounds (VOCs). All samples showed FFA, PV and ?K values within the limits established by law for extra-virgin olive oil. The use of CO<sub>2</sub> did not catalyze hydrolysis, oxidation and condensation of double bonds. Centrifuged oils and oils extracted with carbon dioxide presented the lowest PV and FFA values. Extraction with liquid carbon dioxide contributed to an increasing of phenolic content with a value of 270.5 mg/kg, a value twice that of the oils extracted with centrifugation (135.3 mg/kg) or pressure methods (173.2 mg/kg). Oil extracted with liquid carbon dioxide showed the greatest amount of t-2-octenal and t-2-heptenal, giving herbaceous and pungent notes. Moreover the presence of aromatic compounds such as limonene, generally absent in olive oils, was only detected in the sample extracted with liquid carbon dioxide.</p>


1976 ◽  
Vol 22 (5) ◽  
pp. 633-637 ◽  
Author(s):  
J M Goldberg ◽  
P Pagast

Abstract Results of determination of serum lipase by radial enzyme diffusion correlate well with those by a titrimetric reference method in the abnormal range. The specificity of the diffusion assay allows the differentiation of patients with pancreatic disease, even when the lipase activity of the serum is within the normal limits of the tritrimetric assay. Pancreatic lipase is not detectable by the diffusion assay in the serum of individuals who are free from pancreatic disease.


1976 ◽  
Vol 22 (5) ◽  
pp. 607-610 ◽  
Author(s):  
R D Feld ◽  
D L Witte ◽  
D A Barrett

Abstract A turbidimetric procedure for lipase has been adapted for use on the Abbott Bichromatic Analyzer (ABA-100). The method is rapid and results compared well with those by the more traditional method of Cherry and Crandall [Am. J. Physiol. 100, 266 (1932)]. Advantages of this method include shorter incubation time (2 min), smaller sample size (50 mul), neglible interference from bilirubin, and greater dynamic range (to eightfold normal).


1975 ◽  
Vol 21 (12) ◽  
pp. 1788-1790 ◽  
Author(s):  
Bernd Rietz ◽  
George G Guilbault

Abstract We describe a method for determining lipase (triacylglycerol acyl-hydrolase, EC 3.1.1.3) activity in serum. Emulsified olive oil in tris(hydroxymethyl)aminomethane buffer is used as substrate. The course of the enzymatic reaction is followed by measuring the decrease in fluorescence with time of a fluorescent indicator, 4-methylumbelliferone, added to the substrate, caused by the change in the pH of the substrate solution resulting from the reaction. All measurements are performed at 37 °C. The reaction volume is about 2.3 ml, in a Pyrex cuvette. Change of fluorescence and of enzyme activity are linearly related in the range of 77.8 to 389.0 U/liter. An assay can be done in as little as 3 to 5 min, with excellent precision.


1973 ◽  
Vol 19 (4) ◽  
pp. 384-386 ◽  
Author(s):  
Angelo Burlina ◽  
Lauro Galzigna

Abstract A method is described for turbidimetric assay of lipase activity. The substrate is a two-phase emulsion composed of a fairly homogenous dispersion of micelles of either triolein or olive oil. The de-emulsification of the substrate after lipase addition is a true measure of the enzymatic activity. Turbidity change is related to amount of the enzyme by use of a commercial standard, purified lipase from hog pancreas. The quantitative relationship between turbidity change and the number of micelles provides the theoretical basis for this type of assay.


1956 ◽  
Vol 2 (2) ◽  
pp. 75-82 ◽  
Author(s):  
Leitha D Bunch ◽  
Richard L Emerson

Abstract A method for determining serum lipase activity requiring only 4 hours incubation at 37° is given. Olive oil in a phosphate buffer is the substrate. The values found in 57 healthy controls ranged between 0.06 and 0.87 units, with a mean of 0.31 ± 0.17 (S.D.). Some results are given for patients with pancreatitis, miscellaneous pathologic conditions, and healthy controls.


2013 ◽  
Vol 319 ◽  
pp. 513-516 ◽  
Author(s):  
Xiao Jing Liang ◽  
Gui Qing Wen ◽  
Zhi Liang Jiang

Herring sperm DNA (hsDNA) was used to modify 5 nm nanosilver to obtain a hsDNA-nanosilver probe (Ag-hsDNA) for Hg2+. In the presence of Hg2+, it combined with hsDNA to produce Hg2+-hsDNA complexes and to release nanosilver particles, based on formation of stable T-Hg2+-T mismatches. Nanosilver particles aggregated to form larger nanosilver clusters and led the absorption at 412 nm decreased in the pH 6.5 Na2HPO4-NaH2PO4buffer solution and 0.05 mol/L NaCl medium. The decreased absorption (ΔA412nm) is linear to Hg2+concentration in the range of 1.36-10.86μg/L Hg2+, with regress equation of ΔA=0.0987CHg2++0.0624, correlation coefficient of 0.9890, and detection limit of 0.30μg/L Hg2+. The assay was applied to the analysis of Hg2+in wastewater with satisfactory results.


1977 ◽  
Vol 10 (13) ◽  
pp. 1009-1017 ◽  
Author(s):  
Edward G. Janzen ◽  
S. Patricia Burns
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