Solvent and thermal stability, and pH kinetics, of proline-specific dipeptidyl peptidase IV-like enzyme from bovine serum

Ruth, Deborah M.; Buckley, Seamus J; O’Connor, Brendan F.; Ó’Fágáin, Ciarán

doi:10.1016/j.enzmictec.2007.02.007

Cited by 9 publications

(2 citation statements)

References 37 publications

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“…Enzymes that cleave SP [1][2][3][4][5][6][7][8][9][10][11] include members of the serine and metalloprotease families: angiotensin I-converting enzyme, aminopeptidase, neutral endopeptidase, dipeptidyl peptidase IV, and postproline cleaving enzyme. 13,14 Enzymes of these classes require inhibitors with specific affinity for their catalytic sites; therefore, protection of SP [1][2][3][4][5][6][7][8][9][10][11] from enzymatic degradation may require at least 2 inhibitor types. Various degradation products are derived from SP [1][2][3][4][5][6][7][8][9][10][11] and are named in accordance with the amino acids they contain.…”

Section: Kiu Kallikrein Inhibitor Units Lc-ms-msmentioning

confidence: 99%

Effects of sample handling methods on substance P concentrations and immunoreactivity in bovine blood samples

Mosher

Coetzee

Allen

et al. 2014

ajvr

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Objective—To determine the effects of protease inhibitors and holding times and temperatures before processing on the stability of substance P in bovine blood samples. Samples—Blood samples obtained from a healthy 6-month-old calf. Procedures—Blood samples were dispensed into tubes containing exogenous substance P and 1 of 6 degradative enzyme inhibitor treatments: heparin, EDTA, EDTA with 1 of 2 concentrations of aprotinin, or EDTA with 1 of 2 concentrations of a commercially available protease inhibitor cocktail. Plasma was harvested immediately following collection or after 1, 3, 6, 12, or 24 hours of holding at ambient (20.3° to 25.4°C) or ice bath temperatures. Total substance P immunoreactivity was determined with an ELISA; concentrations of the substance P parent molecule, a metabolite composed of the 9 terminal amino acids, and a metabolite composed of the 5 terminal amino acids were determined with liquid chromatography–tandem mass spectrometry. Results—Regarding blood samples processed immediately, no significant differences in substance P concentrations or immunoreactivity were detected among enzyme inhibitor treatments. In blood samples processed at 1 hour of holding, substance P parent molecule concentration was significantly lower for ambient temperature versus ice bath temperature holding conditions; aprotinin was the most effective inhibitor of substance P degradation at the ice bath temperature. The ELISA substance P immunoreactivity was typically lower for blood samples with heparin versus samples with other inhibitors processed at 1 hour of holding in either temperature condition. Conclusions and Clinical Relevance—Results suggested that blood samples should be chilled and plasma harvested within 1 hour after collection to prevent substance P degradation.

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Section: Kiu Kallikrein Inhibitor Units Lc-ms-msmentioning

confidence: 99%

Effects of sample handling methods on substance P concentrations and immunoreactivity in bovine blood samples

Mosher

Coetzee

Allen

et al. 2014

ajvr

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“…This parameter corresponds to the temperature at which the residual activity (Eq. (4)) drops to 50% of its initial value after a brief period of incubation, such as 10 (Ruth et al, 2007) or 15 min (Ó'Fágáin, 1997). The basic profile for this type of analysis would be of a sigmoidal type, where, at a certain temperature, the activity decreases significantly, indicating that a brief incubation is sufficient to affect thed thermal stability of the enzyme.…”

Section: T 50 and Thermal Activationmentioning

confidence: 99%

Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp

Aguiar‐Oliveira

Maugeri

2011

Braz. J. Chem. Eng.

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-The thermal stability of the extracellular fructosyltransferase (FTase) from Rhodotorula sp., recovered from cultivation medium by ethanol precipitation and immobilized onto niobium ore, was studied by Arrhenius plot, half-life profile, half-inactivation temperature (T 50 ) and thermodynamic parameters. The Arrhenius plot showed two different behaviors with different deactivation energies (E ad ) only after immobilization, the transition occurring in the temperature interval between 51 and 52°C. T 50 for the free enzyme was estimated to be around 62°C and, after immobilization, 66°C. After 15 minutes at 52°C, it was also possible to observe enzymatic activation for both the free and immobilized forms, but greater activation was achieved at pH 4.5 with the immobilized enzyme. Between 47-51°C the immobilized enzyme was more stable than the free enzyme, with pH 6.0 being the more stable condition for the immobilized enzyme. However, above 52°C the free form was more stable.

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Aldehyde Oxidase Activity and Stability in Water-Miscible Organic Solvents

Rashidi

Dehghany

Dehghan

et al. 2013

Appl Biochem Biotechnol

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In this study, the catalytic activity of aldehyde oxidase was investigated in various water-miscible organic solvents for the first time. The enzyme was partially purified from rabbit liver, and its activity was determined in the absence/presence of nine hydro-organic mixtures. The effects of pH and temperature on the enzyme activity were also investigated. The activity was reduced in the presence of all nine organic solvents. However, in some cases, the residual activity remained almost unchanged throughout the incubation of enzyme at 35 °C for 24 h. Considering potential advantages of doing reactions in the presence of organic solvents, these results could be of value. The enzyme showed different behavior in the reaction solutions making it difficult to formulate results in a single comprehensive model. The results indicated that binding and cleavage of the substrate are influenced in the presence of organic solvents.

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Solvent and thermal stability, and pH kinetics, of proline-specific dipeptidyl peptidase IV-like enzyme from bovine serum

Abstract: SummaryProline-specific dipeptidyl peptidase-like (DPP IV; EC 3.4.14.5)

Cited by 9 publications

References 37 publications

Effects of sample handling methods on substance P concentrations and immunoreactivity in bovine blood samples

Effects of sample handling methods on substance P concentrations and immunoreactivity in bovine blood samples

Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp

Aldehyde Oxidase Activity and Stability in Water-Miscible Organic Solvents

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