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- Module Code & Title: CHM9011M Chromatography and Sep Sciences Section 1: Purpose Clarity of Purpose ): Clearly states the purpose of the SOP. Relevance to Task : Demonstrates the importance and relevance of the procedure. Alignment with Goals ): Shows how the procedure aligns with organisational goals.Calculate the values of vrms, vmp, and vmean for Cl2 (70.90 g mol-1) at 25 °CWrite the Lineweaver–Burk (doublereciprocal) equation and describe thefeatures of a Lineweaver–Burk plot.
- 5 0.0030 0.0015 0.0005 6 0.0030 0.0057 0.0089 7 0.0086 0.0057 0.0089 Show the Calculations of Qc and Kc for Exp. 5-7 Please help me out. ThanksFrom the equivalent conductivities at infinite dilution following at 18°C, find the value of Λ° for NH4OH:Ba(OH)2 Λ° = 228.8BaCl2 Λ° = 120.3NH4Cl Λ° = 129.8Construct the expression for Ksp for solid Ba₃(PO₄)₂ in aqueous solution. Ba₃(PO₄)₂(s) ⇌ 3 Ba²⁺(aq) + 2 PO₄³⁻(aq)
- If the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM, what is its Km? Calculate Vmax of the above enzyme (lactase). Calculate the slope on a Lineweaver-Burk plot (Km/Kmax) for the above enzyme (lactase).Briefly Define Lc-Ms-Ms System? Please answer at your own easy words. Please don't use AI for answering this question.The following experimental data were collected during a study of the catalytic activity of an intestinalpeptidase with the substrate glycylglycine: Glycylglycine + H2O → 2 glycine [S] (mM) Rate of product formation (mol/min) 1.5 0.21 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45 Use the graphical analysis (Lineweaver-Burk plot and equation) to determine the Km and Vmax for this enzyme preparation and substrate.
- Answer Q45, 46 & 47 show-all-working-explaining-detailly-each-step Answer should be typewritten using a computer keyboard.Define the term lambda max (λmax)A wet pipette was used to transfer 10.00 mL of 1M HNO3 in the determination of ΔHrxn. [magnitude of ΔHrxn] In a maximum of 3 sentences explain why ΔHrxn decreases.