Learning Materials
Features
Discover
Chapter 5: Q14CP (page 119)
What types of information can be retrieved from a protein sequence database?
The protein sequence database retrieve protein sequence records by gene name, organism, author name, accession number and a variety of other text terms.
Over 30 million students worldwide already upgrade their learning with 91影视!
All the tools & learning materials you need for study success - in one app.
Get started for free
Consult Table 5-1 to complete the following: (a) On a plot of absorbance at 280 nm versus elution volume, sketch the results of gel filtration of a mixture containing human cytochrome c and bacteriophage T7 RNA polymerase and identify each peak. (b) Sketch the results of SDS-PAGE of the same protein mixture showing the direction of migration and identifying each band.
What fractionation procedure could be used to purify protein 1 from a mixture of three proteins whose amino acid compositions are as follows?
1. 25% Ala, 20% Gly, 20% Ser, 10% Ile, 10% Val, 5% Asn, 5% Gln, 5% Pro
2. 30% Gln, 25% Glu, 20% Lys, 15% Ser, 10% Cys
3. 25% Asn, 20% Gly, 20% Asp, 20% Ser, 10% Lys, 5% Tyr
All three proteins are similar in size and pI, and there is no antibody available for protein 1.
Explain how you would use salting out to prepare a more concentrated solution of a protein.
Question: Purification tables are often used to keep track of the yield and purification of a protein. The specific activity is a ratio of the amount of the protein of interest, in this case Mb, obtained at a given step (渭mol or enzyme units) divided by the amount (mg) of total protein. The yield is the ratio of the amount of the protein of interest obtained at a given step (渭mol or enzyme units) divided by the original amount present in the crude extract, often converted to percent yield by multiplying by 100. The fold purification is the ratio of the specific activity of the purified protein to that of the crude preparation.
(a) For the purification table below, calculate the specific activity, % yield, and fold purification for the empty cells.
(b) Which step鈥擠EAE or affinity chromatography鈥攃auses the greatest loss of Mb?
(c) Which step causes the greater purification of Mb?
(d) If you wanted to use only one purification step, which technique would you choose?
You are trying to purify a protein that is soluble in a solution of 2 M ammonium sulfate. After centrifugation to remove other proteins that have precipitated at this high salt concentration, you recover the supernatant to assay the target protein鈥檚 activity in a cell culture system.
(a) Explain why the cells die when incubated with the supernatant.
(b) What procedure could you perform to correct the problem? (Hint: See Section 2-1D).
What do you think about this solution?
We value your feedback to improve our textbook solutions.
Explanations 
Textbooks 
Flashcards 
91影视 AI 
Notes 
Study Plans 
Study Sets 
Find a degree 
Magazine