scholarly journals Determination of lipase activity in AOT-isooctane reversed micelles.

1987 ◽  
Vol 51 (2) ◽  
pp. 615-618 ◽  
Author(s):  
Daeseok HAN ◽  
Dae Young KWON ◽  
Joon Shick RHEE
Keyword(s):  
Lipase Activity ◽  
Reversed Micelles

Determination of Lipase Activity in AOT-Isooctane Reversed Micelles

1987 ◽  
Vol 51 (2) ◽  
pp. 615-618 ◽  
Author(s):  
Daeseok Han ◽  
Dae Young Kwon ◽  
Joon Shick Rhee
Keyword(s):  
Lipase Activity ◽  
Reversed Micelles

Electrochemical determination of lipase activity in pharmaceutical preparations

2000 ◽  
Vol 45 (18) ◽  
pp. 2933-2937 ◽  
Author(s):  
Tetsuo Fuse ◽  
Go Oda ◽  
Kensuke Arai ◽  
Kiyoko Takamura ◽  
Fumiyo Kusu
Keyword(s):  
Lipase Activity ◽  
Pharmaceutical Preparations ◽  
Electrochemical Determination

A software package to streamline the titrimetric determination of lipase activity

1995 ◽  
Vol 72 (11) ◽  
pp. 1405-1406 ◽  
Author(s):  
Michael J. Haas ◽  
Dominic Esposito ◽  
David J. Cichowicz
Keyword(s):  
Lipase Activity ◽  
Software Package ◽  
Titrimetric Determination

Evaluation of lipase activity in serum by radial enzyme diffusion.

1976 ◽  
Vol 22 (5) ◽  
pp. 633-637 ◽  
Author(s):  
J M Goldberg ◽  
P Pagast
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Reference Method ◽  
Pancreatic Disease ◽  
Serum Lipase ◽  
Normal Limits ◽  
Diffusion Assay

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.

Kinetic determination of serum lipase activity with the Abbott ABA-100.

1976 ◽  
Vol 22 (5) ◽  
pp. 607-610 ◽  
Author(s):  
R D Feld ◽  
D L Witte ◽  
D A Barrett
Keyword(s):  
Sample Size ◽  
Lipase Activity ◽  
Incubation Time ◽  
Traditional Method ◽  
Dynamic Range ◽  
Serum Lipase ◽  
Kinetic Determination

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).

scholarly journals Indoxyl Acetate as a Substrate for Analysis of Lipase Activity

2019 ◽  
Vol 2019 ◽  
pp. 1-7
Author(s):  
Tomas Valek ◽  
Adam Kostelnik ◽  
Pavla Valkova ◽  
Miroslav Pohanka
Keyword(s):  
Analytical Chemistry ◽  
Reaction Time ◽  
Standard Method ◽  
Lipase Activity ◽  
Calibration Curve ◽  
Heart Diseases ◽  
Similar Reaction ◽  
Activity Determination ◽  
Menten Constant

Lipases play a crucial role in metabolism of microbes, fungi, plants, and animals, and in analytical chemistry, they are often used in detection of fats and triglycerides. Determination of lipase activity is also important in toxicology, when lipase activity can be both increased and decreased by organophosphates and other pesticides and in medicine for diagnosis of heart diseases. The standard method for lipase activity determination is based on cleaving ester bonds in lipase buffer containing Tween. Our aim was to find a method with faster and more sensitive response. It is known that acetylcholinesterase belongs to the same group of hydrolases enzymes as lipases and it cleaves indoxyl acetate, so we assume indoxyl acetate could report a similar reaction with lipase. Our method is based on indoxyl acetate as a substrate for lipase, where indoxyl acetate is cleaved by lipase to indoxyl and acetate moiety and blue indigo is created. The method was optimized for different times and amount of enzyme and compared with the standard Tween assay. The calibration curve measured in reaction time 20 minutes with 10 μl of lipase exhibited the best analytical parameters, and it showed Michaelis–Menten response with the Michaelis–Menten constant equal to 8.72 mmol/l. The indoxyl acetate-based method showed faster and more sensitive response than the standard method for lipase activity determination, so it has great potential in biosensor construction and it could be used in industry, medicine, toxicology, and common practice where the activity of lipases is need to be measured.

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