Selective functional activity measurement of a PEGylated protein with a modification-dependent activity assay

2017 ◽  
Vol 132 ◽  
pp. 207-214 ◽  
Author(s):  
Alfred Weber ◽  
Andrea Engelmaier ◽  
Gabriele Mohr ◽  
Sonja Haindl ◽  
Hans Peter Schwarz ◽  
...  
Keyword(s):  
Functional Activity ◽  
Activity Measurement ◽  
Activity Assay ◽  
Dependent Activity ◽  
Pegylated Protein

The Voltammetric Study of β–Glucosidase Hydrolytic Product with Modified Electrode

2016 ◽  
Vol 675-676 ◽  
pp. 671-674
Author(s):  
Chariwat Pitsanuwong ◽  
Sumamal Charernchai ◽  
Wanida Wonsawat
Keyword(s):  
Modified Electrode ◽  
Enzyme Purification ◽  
Activity Measurement ◽  
The Novel ◽  
Activity Assay ◽  
Enzyme Activity Assay ◽  
Hydrolytic Product ◽  
Voltammetric Study ◽  
Screen Printed Carbon Electrode ◽  
Voltammetric Technique

The novel modified electrode of voltammetric technique was applied to detect p-nitrophenol quantity released from the synthetic substrate p-nitrophenyl-β-D-glucopyranoside (pNPG) for β-glucosidase activity measurement. The results from the developed bismuth film modified screen printed carbon electrode (Bi/SPCE) for p-nitrophenol detecting, can be used for enzyme activity assay during purification steps. The further work, the condition of convenient voltammetric method will be optimized the condition suitable for applying to the β-glucosidase enzyme purification from Terminalia ivorensis C. seeds.

Representing utility and deploying the body

2020 ◽  
Vol 43 ◽  
Author(s):  
David Spurrett
Keyword(s):  
Functional Activity ◽  
Degrees Of Freedom ◽  
The Body ◽  
Target Article ◽  
Processing Demands ◽  
The Many

Abstract Comprehensive accounts of resource-rational attempts to maximise utility shouldn't ignore the demands of constructing utility representations. This can be onerous when, as in humans, there are many rewarding modalities. Another thing best not ignored is the processing demands of making functional activity out of the many degrees of freedom of a body. The target article is almost silent on both.

Azocoll protease activity assay

2007 ◽  
Author(s):  
Naxin Jiang ◽  
Nguan Soon Tan ◽  
Bow Ho ◽  
Jeak Ling Ding
Keyword(s):  
Protease Activity ◽  
Activity Assay

Plasma Derived von Willebrand Factor Preparations: Collagen Binding and Ristocetin Cofactor Activities

1997 ◽  
Vol 78 (02) ◽  
pp. 930-933 ◽  
Author(s):  
Ping Chang ◽  
D L Aronson
Keyword(s):  
Von Willebrand Factor ◽  
Functional Activity ◽  
Binding Activity ◽  
Collagen Binding ◽  
Binding Function ◽  
Cofactor Activity ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Ristocetin Cofactor ◽  
Ristocetin Cofactor Activity

SummaryFive plasma preparations (11 lots) used in the treatment of von Willebrand’s disease (vWD) were evaluated. The collagen binding function of von Willebrand factor (vWF) containing preparations was compared with the ristocetin cofactor activity and the vWF antigen. Some preparations have higher ratio of functional activity (ristocetin cofactor and collagen binding) relative to the antigen than is found in normal plasma. The ristocetin cofactor activity and the collagen binding activity are tightly correlated (r = .95). Ultracentrifugal (UCF) analysis was used to compare the size distribution of vWf antigen, ristocetin cofactor and collagen binding activity. The sedimentation of all of the vWF parameters in the plasma products was slower than in plasma. In plasma products the ristocetin cofactor activity sediments the most rapidly, the collagen binding activity is slower and the antigen the slowest. The collagen/antigen ratio decreases with decreasing vWF size. Assignment of potency to vWF containing preparations utilizing the collagen binding activity may be more precise and as accurate as with the traditional ristocetin cofactor assay.

Determination of Factor XIII Activity and of Factor XIII Inhibitors Using an Ammonium-Sensitive Electrode

1983 ◽  
Vol 50 (02) ◽  
pp. 563-566 ◽  
Author(s):  
P Hellstern ◽  
K Schilz ◽  
G von Blohn ◽  
E Wenzel
Keyword(s):  
Factor Xiii ◽  
Normal Subjects ◽  
The Other ◽  
Activity Measurement ◽  
Factor Xiii Deficiency ◽  
Assay Procedure ◽  
Stabilization Factor ◽  
Release Method ◽  
Sensitive Electrode

SummaryAn assay for rapid factor XIII activity measurement has been developed based on the determination of the ammonium released during fibrin stabilization. Factor XIII was activated by thrombin and calcium. Ammonium was measured by an ammonium-sensitive electrode. It was demonstrated that the assay procedure yields accurate and precise results and that factor XIII-catalyzed fibrin stabilization can be measured kinetically. The amount of ammonium released during the first 90 min of fibrin stabilization was found to be 7.8 ± 0.5 moles per mole fibrinogen, which is in agreement with the findings of other authors. In 15 normal subjects and in 15 patients suffering from diseases with suspected factor XIII deficiency there was a satisfactory correlation between the results obtained by the “ammonium-release-method”, Bohn’s method, and the immunological assay (r1 = 0.65; r2= 0.70; p<0.01). In 3 of 5 patients with paraproteinemias the values of factor XIII activity determined by the ammonium-release method were markedly lower than those estimated by the other methods. It could be shown that inhibitor mechanisms were responsible for these discrepancies.

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