Question

Immunoprecipitation is a variation of what type of protein purification method? Choose one: O A. Affinity chromatography O B.
0 0
Add a comment Improve this question Transcribed image text
Answer #1

Immunoprecipitation is a variation of what type of protein purification method-

Answer- A. Affinity chromatography

In immunoprecipitation, a particular protein antigen is separated from the pool of other antigens.

Affinity chromatography separates a particular substance from a mixture solution based on the affinity.

In gel electrophoresis separation is based on charge and size.

Please give a thumbs up!!!!!!!! Ask any doubts regarding the above question in the comment section !!!!!!!!!!! Thank you!!!!!

Add a comment
Know the answer?
Add Answer to:
Immunoprecipitation is a variation of what type of protein purification method? Choose one: O A. Affinity...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions
  • 4.     (Challenge) You are purifying a protein from the brain of patients with an unusual type of...

    4.     (Challenge) You are purifying a protein from the brain of patients with an unusual type of dementia triggered by a coronavirus and you hypothesize that this protein may be a signature molecule of this type of dementia. To pursue this hypothesis, you collect brain tissue from patients post mortem, do differential centrifugation, density gradient centrifugation, CM (carboxymethyl cellulose) ion exchange chromatography and gel filtration. You then assess the purity of your protein using both native and SDS gel electrophoresis. The...

  • Based on the discussed protein purification/characterization techniques which chain of experiments makes logical sense if one...

    Based on the discussed protein purification/characterization techniques which chain of experiments makes logical sense if one wants to study protein structure? a. Cell/tissue homogenization->Affinity chromatography->Mass-Spec-> Gel filtration chromatography b. Cell/tissue homogenization->Mass-Spec->Gel filtration chromatography->Affinity chromatography c. Cell/tissue homogenization->Gel filtration chromatography->Affinity chromatography->Mass-Spec d. Gel filtration chromatography->Cell/tissue homogenization->Affinity chromatography->Mass-Spec

  • Can someone answer the question and provide a short explanation? Thanks! Which of the following statements...

    Can someone answer the question and provide a short explanation? Thanks! Which of the following statements is NOT correct regarding protein seperation techniques? A) Size-exclusion chromatography works on the same principle as polyacrylamide gel electrophoresis B) Specific antibodies are required for immunoblotting, antibody affinity chromatography as well as immunoprecipitation C) Two-dimensional gel electrophoresis is conceptually the same as combining gel filtration chromatography and ion exchange chromatography D) Western blotting is a useful technique to isolate proteins for use in downstream...

  • a-d plz 7. Protein purification. As a graduate student, the first protein I purified was RNA...

    a-d plz 7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP) from E. coli- Some physical and chemical properties of Ecoli RNAP Molecular max470,000 g/mol polynentide compasitian (subunits): (50 kDa), k andok a pl = 5.34 substrates: NTPs cofactor: Mg? Purification protocol. E coli cells were broken usine Isozyme, yielding a cellualar extract containing a protcome solution 4M (NHOSO, was added to the cellular extract. A white protein precipitate was formed incuding RNAM...

  • 7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP)...

    7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP) from E. coli. Some physical and chemical properties of E. coli RNAP Molecular mass = 470,000 g/mol polypeptide composition (subunits): a (50 kDa), B (150 kDa) and 6 (70 kDa) pl = 5.34 substrates: NTPS cofactor: Mg Purification protocol. E. coli cells were broken using lysozyme, yielding a cellualar extract containing a proteome solution. 4M (NH4)2SO4 was added to the cellular extract. A white...

  • You would like to purify protein A (pI=6.0, MW=32 kDa) from a mixture that also contains...

    You would like to purify protein A (pI=6.0, MW=32 kDa) from a mixture that also contains protein B (pI=6.0, MW 32 kDa) and peptide C (pI=5.5, MW= 3 kDa). Which one of the following techniques would give you the best possible result? a) High Pressure Liquid Chromatography (HPLC) b) Gel Filtration c)Ion Exchange d)Affinity Chromatography e) SDS-PAGE

  • 16) At which pH values would two different peptides, one with a pl of 5.9 and...

    16) At which pH values would two different peptides, one with a pl of 5.9 and the other with a pl of 9.1, both bind to a cation exchange column? A) pH 3.9 B) pH 7.3 C) pH 10.9 D) None of the above 17) Which type of gel matrix (aka resin) would separate the following proteins using size exclusion chromatography: protein 1 (2,000 Da), protein 2 (7,000 Da), protein 3 (20,000 Da), and protein 4 (90,000 Da)? A) Gel...

  • By which purification method are proteins purified based on their net charge? 4 Preparative centrifugation Dialysis...

    By which purification method are proteins purified based on their net charge? 4 Preparative centrifugation Dialysis Affinity chromatography Gel filtration size exclusion lon exchange chromalography three-leter abbreviation Glu sienifies which amino acid? Glucose Glycine Glucagon Glutamine Glutamicacid 6 The function of glycosyltransferases is to? Convert hex oses to hexosamines Break down structural carbohydrates such as cellulose and chitin 0 Covalently link monosaccharides to other carbohydrates or to proteins ides from the Golgi apparatus to the plasma membrane

  • Combined chromatography methods You are provided with a solution containing a mixture of three different proteins...

    Combined chromatography methods You are provided with a solution containing a mixture of three different proteins with the following characteristics. Protein mol. mass (Da) isoelectric point (pI) Binds to ligand? A 45,000 6.1 Yes B 84,000 7.8 No C 85,000 7.9 Yes D 120,000 6 No E 122,000 8.0 No You are also provided with a size exclusion column, an ion-exchange column, and an affinity purification column (containing the ligand recognised by proteins A and C above). With the information...

  • 1) You are faced with separating two different proteins with identical mass. Protein A is a...

    1) You are faced with separating two different proteins with identical mass. Protein A is a rod-like molecule with a great deal of secondary srtucture and protein B is a globular protein that is roughly spherical. What methods could be used to separate these two proteins? (check all that apply). A. Ion-exchange chromatography B. Two-dimensional electrophoresis C. SDS PAGE D. Size exclusion chromatography E. Affinity chromatography

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT