enzyme kinetic module of sigmaplot version 9.01 (SYSTAT)
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Enzyme Kinetic Module Of Sigmaplot Version 9.01, supplied by SYSTAT, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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other:Article Title: Naturally occurring monoepoxides of eicosapentaenoic acid and docosahexaenoic acid are bioactive antihyperalgesic lipids Article Snippet: The kinetic constants (K M and V m ) were calculated by nonlinear fitting of the Michaelis equation using the enzyme kinetic module of Article Title: Naturally occurring monoepoxides of eicosapentaenoic acid and docosahexaenoic acid are bioactive antihyperalgesic lipids Article Snippet: The kinetic constants (K M and V m ) were calculated by nonlinear fitting of the Michaelis equation using the enzyme kinetic module of Article Title: Naturally occurring monoepoxides of eicosapentaenoic acid and docosahexaenoic acid are bioactive antihyperalgesic lipids Article Snippet: The kinetic constants (K M and V m ) were calculated by nonlinear fi tting of the Michaelis equation using the enzyme kinetic module of Article Title: Naturally occurring monoepoxides of eicosapentaenoic acid and docosahexaenoic acid are bioactive antihyperalgesic lipids Article Snippet: The kinetic constants (K M and V m ) were calculated by nonlinear fi tting of the Michaelis equation using the enzyme kinetic module of Standard Deviation:Article Title: Role of soluble epoxide hydrolase phosphatase activity in the metabolism of lysophosphatidic acids Article Snippet: .. The kinetic constants (K M and V M ) were calculated by non-linear fitting of the Michaelis equation using the enzyme kinetic module of Activity Assay:Article Title: Effect of soluble epoxide hydrolase polymorphism on substrate and inhibitor selectivity and dimer formation Article Snippet: .. Based on the recently reported observation that only the dimer is active ( 16 ), the dimer/monomer dissociation constant ( K D/M ), the amount of |
![Determination of the kinetic constants for 14,15-EpETE (A) and 13,14-EpDPE (B) with the human sEH([E]final ≈ 3 nM) in Bis-Tris HCl buffer (25 mM, pH 7.0) containing 0.1 mg/ml of lipid free BSA at 30°C. The kinetic constants (KM and Vm) were calculated by nonlinear fitting of the Michaelis equation using the enzyme kinetic module of SigmaPlot version 9.01 (Systat Software Inc., Chicago, IL).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_5720/pmc02975720/pmc02975720__3481fig1.jpg)