Influence of Colipase on the Turbidimetric Determination of Pancreatic Lipase Catalytic Activity

Junge, Wolfgang; Leybold, K.; Kraack, Barbara

doi:10.1515/cclm.1983.21.7.445

Cited by 9 publications

(5 citation statements)

References 13 publications

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“…3). Colipase at 0.2 mg/1 appeared to enhance maximally the enzyme activity in most cases; differences in the degree of activation may be attributed to the presence of various amounts of endogenous colipase in human plasma, äs already suggested by Junge et al (15).…”

Section: Effectorssupporting

confidence: 54%

Transferability of Lipase Titrimetric Assays: Deductions from an Interlaboratory Study

Arzoglou¹,

Goudoula²,

Tsantili³

et al. 1994

Clinical Chemistry and Laboratory Medicine

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Following the selection of the most appropriate method for emulsification and the optimization of the reaction medium, interlaboratory studies were conducted to check the effect of preparing Substrates and measuring the catalytic concentration of lipase at different sites äs well äs the effect of transport on emulsion. The determinations of lipase activity in an abnormal chemistry control against emulsions prepared by two laboratories (and used by both laboratories) and, also, against five separate emulsions prepared by one laboratory (and used by five different laboratories) resulted in average enzyme activity vahies (2234 ±125 and 2263 ± 204 U/l respectively) which are not statistically different. Standard preparations of lipase, control sera and reference materials can therefore be titrated according to the procedure followed by at least two laboratories for at least 3 days against two separate emulsions. Introduction(6-11). Differences between the assay procedures hitherto described are related to < he c ™P ositi ™ of the reacFor decades, the unique properties of pancreatic lipase (EC 3.1.1.3) have sustained a controversy over the tlon mixture ^& ^P e ™ d ^ncentration of bile salt) method and the in vitro conditions for reliable.determin-and the *W* of emulsification procedure employed. Owations of the enzyme catalytic concentration (l -4). The in § to * e multitude of emulsification devices, there is a most widely used routine indkect turbidimetric method g^at Variation in the physical state of Substrates, which (5) requires the prior direct assay of Standards and, in turn affects the expression of lipase activity, thus hinmoreover, is restricted to low Substrate concentrations, dering the comparability of results obtained by difowing to the limitations of spectrophotometry (2, 4). The ferent laboratories. latest titrimetric assays, which make use of continuousmonitoring pH-stat techniques for direct titration of the Within the context of this work, an effort was made to released fatty acids, offer a satisfactory approach to the deal with some of the main factors involved in the prepproblern, because they allow the use of high Substrate aration of Substrates and to subject the whole titrimetric concentrations while photometric artefacts are excluded procedure to an interlaboratory study.

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Section: Effectorssupporting

confidence: 54%

Transferability of Lipase Titrimetric Assays: Deductions from an Interlaboratory Study

Arzoglou¹,

Goudoula²,

Tsantili³

et al. 1994

Clinical Chemistry and Laboratory Medicine

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“…The method was modified from the assay reported by Junge et al , in which triolein was used as a substrate to measure the pancreatic lipase inhibitory activity of all samples. Briefly, the reaction mixture (3.06 mL) containing 135 mM triolein emulsified in sodium thioglycolate, lipase (0.4 U) and the sample was adjusted to pH 8.8, incubated at 25°C.…”

Section: Methodsmentioning

confidence: 99%

Synthesis and Evaluation of New Bis‐1,3,4,2‐triazaphospholinoalkane Derivatives as In Vitro α‐Amylase and Lipase Inhibitors

Hamzaoui

Salah

Hamden

et al. 2015

Archiv der Pharmazie

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A series of new 1,ω-bis-(5-alkyl-2-oxide-3-tosyl-1,3,4,2-triazaphospholino)alkanes 2 and 3 were prepared in good yields by the treatment of 1,ω-bis-(1-tosylamidrazone)alkanes 1 with two molar equivalents of phosphoryl trichloride and phenylphosphonic dichloride, respectively. All the newly synthesized compounds were characterized by IR, (1) H NMR, (13) C NMR, (31) P NMR, and elemental analysis. All the new compounds were screened for their inhibitory effect on the key enzymes related to diabetes and obesity, as α-amylase and lipase. The in vitro study revealed that these alkane derivatives exert an inhibitory action against these key enzymes, especially 2b with an IC50 of 16 μg/mL against α-amylase and lipase. Overall, the findings of the current study indicate that 2d exhibits attractive properties and can therefore be considered for future application in the development of antidiabetic and hypolipidemic drugs.

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“…The method was modified from the assay reported by Junge et al 17, in which triolein was used as a substrate to measure the pancreatic lipase inhibitory activity of all samples. Briefly, the reaction mixture (3.06 mL) containing 135 mM triolein emulsified in sodium thioglycolate, lipase (0.4 unit) and the sample was adjusted to pH 8.8, incubated at 25°C.…”

Section: Methodsmentioning

confidence: 99%

Synthesis and Evaluation of 1,ω‐Bis(1,2,3,5‐thiatriazol‐5‐yl)alkanes as In Vitro and In Vivo α‐Amylase and Lipase Inhibitors

Hamzaoui

Hamden

Salem

et al. 2013

Archiv der Pharmazie

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Thionyl chloride reacts with 1,ω-bis-(1-tosylamidrazone)alkanes 1 to give a series of 1,ω-bis-(4-alkyl-2-tosyl-1,2,3,5-thiatriazol-5-yl)alkanes 2. All the newly synthesized compounds were characterized by IR, 1H NMR, 13C NMR, elemental analysis, and ESI-MS spectral data. All the new compounds were screened for their inhibitory effect on key enzymes related to diabetes and obesity, such as α-amylase and lipase. In vitro and in vivo studies revealed that these thiatriazole derivatives exert an inhibitory action against these key enzymes. Moreover the administration of these compounds to surviving diabetic rats induced a significant decrease in plasma glucose level. Additively 2d significantly protected the liver-kidney functions and modulated lipid metabolism, which were evidenced by the decrease in aspartate transaminase (AST), alanine transaminase (ALT), and gamma-glutamyl transpeptidase (GGT) activities and creatinine, urea albumin, LDL-cholesterol and triglycerides levels as well as an increase in the HDL-cholesterol level in surviving diabetic rats. Overall, the findings of the current study indicate that 2d exhibits attractive properties and can, therefore, be considered for future application in the development of anti-diabetic and hypolipidemic drugs.

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Influence of Colipase on the Turbidimetric Determination of Pancreatic Lipase Catalytic Activity

Cited by 9 publications

References 13 publications

Transferability of Lipase Titrimetric Assays: Deductions from an Interlaboratory Study

Transferability of Lipase Titrimetric Assays: Deductions from an Interlaboratory Study

Synthesis and Evaluation of New Bis‐1,3,4,2‐triazaphospholinoalkane Derivatives as In Vitro α‐Amylase and Lipase Inhibitors

Synthesis and Evaluation of 1,ω‐Bis(1,2,3,5‐thiatriazol‐5‐yl)alkanes as In Vitro and In Vivo α‐Amylase and Lipase Inhibitors

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