Answered: An antibody X binds to an antigen Y.…

An antibody X binds to an antigen Y. When the antigen concentration is 3.0 x 10 M, 0 is 0.50. What is the dissociation constant, Kg, of the antibody for the antigen? Ka =

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter31: Immunochemistry

Section: Chapter Questions

Problem 31.60P

See similar textbooks

Related questions

Q: Subtilisin is a protease that is often added to laundry detergents to help remove protein-based…

Q: The catalytic activity of an insect aminopeptidase was investigatedusing an artificial peptide…

A: Enzymes are known as bio-catalyst. They enhance the reactions taking place inside our body. Enzyme…

Q: The three pKa values for this amino acid slycine are 1.9, 7.5, and 10.8. Calculate the isoelectric…

A: The isoelectronic point is the pH at which the amino acid exist in zwitter ion form.

Q: Hemoglobin A has a pI value of 5.6 whereas the variant hemoglobin M has an aspartate residue in…

Q: In what buffer system (PAH, SAD, or DOH) will Phoebe store the enzyme? (show calculations and…

A: The pH of a buffer solution can be determined by Henderson's equation given below. pH=pKa +…

Q: Draw the structures of the amino acids phenylalanine and aspartate in the ionization state you would…

A: We have been asked to draw the structures of phenylalanine and aspartate at pH = 7 We have been…

Q: viii) You have the following stock solutions available: 2.5M Tris, 0.5M Glycine and 10% SDS, how…

A: To prepare 1 liter solution of 25mM tris, 190mM glycine and 0.1% SDS can be prepared by following.

Q: 4) In the lab you are extracting and enzyme called catalase from a potato and want to use this…

A: Enzymes are commonly help in speed up the reaction. Catalase is an enzyme that is found in almost…

Q: The concentration of a biomolecule inside a rod-shaped prokaryotic cell is 0.0043M. Calcuate the…

A: Solution stoichiometry involves the calculation of concentration of solutions in the given…

Q: Chemistry How do I calculate the %ionisation at pH of a drug (compound code;UQPC 22-606-Q) the “Q”…

A: percent ionization = [H+]/[unionized form ] ×100

Q: Which of the following tetrapeptides will be retained on a cation-exchange column at pH 8.2? O HGTH…

A: Ion exchange chromatography separates ions and molecules based on their net overall surface charge.…

Q: 2. At about 26,000 feet, if the partial pressure of oxygen is about 30 torr, what is the fractional…

A: given: partial pressure of O2 = 30 torr P50 = 26 Hill coefficient of hemoglobin n = 3 fractional…

Q: Consider an amino acid with the following pKa values: pKa1 = 2.71 and pK, = 9.31 At what pH value in…

A: Amino acids are amphoteric in nature due to the presence their ionizable α-amino and α-carboxylic…

Q: Which one of the following methods is not usually used for the analysis of synthetic colorants: a.…

A: soltuion is shown below

Q: Show how the composition of an aqueous solution that contains 20 mmol dm-3 glycine varies with pH .…

A: Given data: [H3N-CH2-COOH] = 20 mmol dm-3 pKa1 = 9.60 pKa2 = 2.35 Calculation of Ka1 and Ka2: pKa1 =…

Q: The electrophoresis of a sample containing 2-amino-4-methylpentanoic acid. (pKa of a-COOH = 2.2, pKa…

Q: What is responsible for the large range in values of dissociation constants listed in Table 2.18?

A: In the above given types of bio affinity interactions there are different types of intermolecular…

Q: An enzyme reaction takes place in a 10mL solution that has a total citrate concentration of 120mM…

A: Part (a)Citric acid is a triprotic acid. Since the value of initial pH is higher than pKa3, the…

Q: The Ksp of BaSO4 is 1.7 x 10-10. Calculate the concentration of the Ba+2 and SO4-2.

A: Since you have posted multiple questions, we will solve first one for you. To get remaining…

Q: The isoelectric point (pl) of a peptide is the pH at which the Group pK peptide ceases to migrate in…

Q: X Incorrect. For 10PF, how would the removal of residues 114-131 affect solute selectivity, assuming…

Q: they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively.…

A: For comparison association constant of each is determined. The one having highest value of…

Q: 4. Why is the following relationship valid? heathte-heat.ater 5. What is the effect of increased…

A: We’ll answer the first question since the exact one wasn’t specified. Please submit a new question…

Q: The enzyme phosphomannomutase (PMM) binds to phosphate as part of its mechanism to phosphorylate…

A: Since you have asked multiple questions, we will solve the first question for you. If you want any…

Q: 7. If the equilibrium constant of binding of NADH to an enzyme [E] is 2.7=2,7 v Ko =…

A: The concentration of E is calculated in the unit of molar as follows:

Q: Two phenylalanine residues are separated by 1.0 nm in a polypeptide. Calculate the dispersion…

A: Dispersion force is the force of attraction that exist between atoms or molecules that developed…

Q: Arginine is an amino acid which has the following pKa values: pK1: 2.17, pK2: = 9.04, pKR = 12.48.…

A: So, the net charge of arginine at pH = 4 will be +1.

Q: Arginine has ionizable groups with pKa values of 2.17, 9.04, and 12.48. A researcher makes up 73 mL…

A: From the pKa values of arginine, it can be stated that, at pH 8.5 second proton is partially…

Q: What is the key feature of a dialysis bag needed for it to be useful for measuring the binding…

A: Answer - Equilibrium dialysis is useful for measuring small molecule binding to macromolecule . It…

Q: How would changing the enzyme concentration affect Km and Vmax

A: In Enzyme catalysis, the enzyme is used as the catalyst to increase the rate of the reaction without…

Q: Two compartments are separated by a semi- permeable membrane. In the left hand compartment is the…

Q: Given: Alanine: pKa=4 Pkb=9 Histidine: pKa=2 pKb=6 and pKc=9 Taking the structure of the amino…

Q: Temperature 4 °C 21 °C 30 °C 37 °C 90 °C Absorbance at zero min 1.300 0.952 0.876 0.914 0.903…

A: As per Beer-Lambert's law, A=εbcwhere,A=Absorbanceε=Extinction coefficient (in M-1.cm-1)b=path…

Q: The hydronium ion concentration in a solution of an unknown weak acid is 5.77 x 1011. What is the…

A: Pka value is depends upon concentration of H+ ions in the solution.

Q: Determine the buffer capacity of Alanine and Histidine at pH 2.0 and 6.0 respectively and discuss…

A: For the alanine, the value for pKa is 2.34. Now the salt to amino acid ratio to achieve the pH of…

Q: If a drug binds to a receptor with an association rate (kon) of 2 10 moi Ls and a dissociation rate…

Q: The substrate dissociation constant, Ks, is k.1/k1. What do large values of this constant mean? That…

Q: Some Protein P binds to 1 molecule of X. The fractional binding curve (θ vs. [Ligand]) shows that θ…

A: For binding of ligand to a protein, the fractional saturation (θ) is calculated using Hill equation:…

Q: Would the continuous assay of Alkaline phosphatase (kinetics lab) with PNPP as a substrate work if…

Q: Calculate the pH of a 0.100 M alanine (HL/intermediate form) solution. pKb1 = 4.29 and pKb2 =11.67.

Q: Is the inhibitor competitive, uncompetitive or non competitive and why?

A: Competative inhibiton- The inhibitor Binds only free enzyme. Binding occur only free enzyme. Non…

Q: Arginine has ionizable groups with pKa values of 2.17 9.04, and 12.48. A researcher makes up 73 mL…

A: The question is based on the concept of PH. It involves calculation for amino acid Arginine. we…

Q: The recommended working buffer for the restriction enzyme Notl is compe 10 mM MgCh 100 mM NACI 50 mM…

A: Tris HCl is an organic compound often used in buffer solutions such as TAE or TBE for…

Q: At what pH will the amino group of threonine be 50% deprotonated? The pKa values of threonine are…

A: If an acid is exactly 50% disocciated in aqueous solution, then the concentration of A- is equal to…

Q: Among these protein assays, which work in acidic conditions? a. Biuret assay b. Bicinchoninic acid…

A: Biuret assay works in alkaline medium, with the help of sodium potassium tartrate, it react with…

Q: The pKa values for the α-carboxylic acid and the α-amino acid groups is cysteine are 1.092 and…

Question

An antibody X binds to an antigen Y. When the antigen concentration is 3.0x 10- M, 0 is 0.50.
What is the dissociation constant, Ka, of the antibody for the antigen?
Ka =

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

The dissociation constant has to be calculated.

VIEW

Step 2

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps with 2 images

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.

Similar questions

Compare the activation energy in uncatalyzed reactions and in enzyme-catalyzed reactions.
An antibody X binds to an antigen Y. When the antigen concentration is 8.0× 10–8 M, θ is 0.90. What is the dissociation constant, Kd, of the antibody for the antigen?
Some Protein P binds to 1 molecule of X. The fractional binding curve (θ vs. [Ligand]) shows that θ = ⅓ when [X] = 6 mM. What is the Kd for X binding to P?
A dimeric binding protein has a KD1 of 50 nM and a Hill coefficient of 1.4. What is the fraction of the protein that has ligand bound at 17 nM concentration of ligand?
I did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.
How can the Michaelis constant (Km) be identified and used to represent the affinity between the enzyme and the substrate?
You are supplied with the following: NaCl (Mr = 58.443 g/mol) 2.5 M Tris-Cl, pH 8 oplossing / solution (1 Litre) EDTA, sodium salt (Mr = 380.2 g/mol) 10 % Sodium dodecyl sulfate solution Proteinase K solution (50 mg dissolved in 1 ml ddH2O) You need a digestion buffer consisting of the following: 15 mM NaCl 75 mM Tris-Cl, pH 8 16 mM EDTA, pH 8 0.8 % Sodium dodecyl sulfate 0.75 mg/ml proteinase K Calculate: How will you prepare 500 ml of the digestion buffer? Show all your steps and calculations and remember to explain how exactly you will make it up.
How are the target complexes detected in immunoassays used in modern labs? heterogeneous separation labeled Ag or Ab homogeneous separation patient Ab
Hemoglobin A has a pI value of 5.6 whereas the variant hemoglobin M has an aspartate residue in place of the normal valine at position 85 of the alpha chain. What effect will this substitution have on the electrophoretic behavior of the protein at pH 7.0. (explain clearly the reason for your answer)
Calculate the pKb for the following: Novocain, Kb = 7 x10-6 methyl red, Kb = 3 x 10-12 Calculate the pH and % ionization for the following: 0.10 M CH3NH2; pKa = 10.657 0.02 M C6H5NH2; pKa = 4.63
Arginine is an amino acid which has the following pKa values: pK1: 2.17, pK2: = 9.04, pKR = 12.48. Calculate the net charge of arginine at the pH value of 4.
The pKa values of an amino acid are the following: pK1 = 2.18; pK2 = 8.95; pK3 = 10.53, what is the isoelectric point of the amino acid? Show the solution and express the your answer in three significant figures.