4. You have a 1.5 g/mL stock solution of protein. To make 200mL of 15 mg/mL solution, add ANSWER (include unit) of stock and ANSWER (include unit) of water for a final volume of ANSWER (include unit). (HINT: Convert units) This is a 1: ANSWER Dilution. 5. To make 500 milliliters of 1x Buffer, measure ANSWER (include unit) of 4x stock and add ANSWER (include unit) of water to make the total volume ANSWER (include unit). This is a 1: ANSWER Dilution.

4. You have a 1.5 g/mL stock solution of protein. To make 200mL of 15 mg/mL solution, add ANSWER (include unit) of stock and ANSWER (include unit) of water for a final volume of ANSWER (include unit). (HINT: Convert units) This is a 1: ANSWER Dilution. 5. To make 500 milliliters of 1x Buffer, measure ANSWER (include unit) of 4x stock and add ANSWER (include unit) of water to make the total volume ANSWER (include unit). This is a 1: ANSWER Dilution.

Aquaculture Science

3rd Edition

ISBN:9781133558347

Author:Parker

Publisher:Parker

Chapter11: Health Of Aquatic Animals

Section: Chapter Questions

Problem 3KA

See similar textbooks

Similar questions

Protein Solubility 3.5 5 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 pH 15 7.5 1.5 4.5 5 0.027 3 0.042 5.5 5 0.068 0.130 Protein Solubility Versus pH 6 6.5 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 Please provide a brief discussion and explanation of the results. 7.5 7.5 50 0.032 0.053 9 8.5 50 0.054 0.100 21.429%
Protein Solubility 3.5 5.5 5 5 0.068 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.130 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 15 PH 7.5 1.5 4.5 5 0.027 3 0.042 Protein Solubility Versus pH 6.5 6 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 7.5 7.5 50 0.032 0.053 8.5 50 0.054 0.100 21.429% 9 Please provide a brief discussion and explanation of the results. (using isoelectric point and net charge to explain)
can someone explain these calculations to me?
Calculate protein concentration in unknown samples 1, 2, 3: Absorbance of Unknown 1 = 0.541 Absorbance of Unknown 2 = 0.85 Absorbance of Unknown 3 = 1.02 Standard Curve: Y = 0.0073x
I’m stu k in both question please Q 1. To make 500 mL of 1x Buffer, measure ANSWER mL of 10x stock and add ANSWER mL water to make the total volume ANSWER mL. This is a 1: ANSWER Dilution. Q2 You have a 1 g/mL stock solution of protein. To make 100mL of 200 mg/mL solution, add ANSWER mL of stock and ANSWER mL of water for a final volume of ANSWER mL. (HINT: Convert units)
Hd 12 10 8 CO 6 st 4 2 0 0 0.5 not text. only, no text. only, no text. 1 1.5 NaOH Equivalents 2 2.5 You create this titration curve of an amino acid. How many buffering zones are there? Enter a number, no letters. 3 A What is the pka1 of this amino acid? Enter only digits What is the pka2 of this amino acid? Digits A A/ What is the pl of this amino acid? Digits A/
You had a second solution with an unknown concentration of Protein X that had to be diluted 4x before you could measure the absorbance. The diluted solution had an absorbance of 0.76. What is the concentration of the diluted solution in ug/ml and what is the concentration of the original solution
To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?
Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, size exclusion chromatography is being done. Use the graph below and analytical methods to determine molecular weight of protein.
Please answer the question below and show all your work. You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole^-1 cm^-1 Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20- fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution?
1. complete the table below: Volume Procedure (mL) Crude 120 extract GFC 20 IEX 10 Protein Total Unit Total Specific content protein Activity Activity Activity (mg/mL) (mg) (U/mL) (U) (U/mg) 20 (a) (d) 0.356 (h) 11 (b) (e) 0.207 (i) 9 (c) (f) (g) (j) % Purification Recovery fold (k) (1) (n) (m) (0)
True'and false please with brief explanation.