Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 11, Problem 37P
Interpretation Introduction
Interpretation:
The use of the technique of affinity chromatography to purify lectins needs to be explained.
Concept introduction:
Lectin is a protein that can recognize carbohydrates and can bind to them. Affinity chromatography is a technique that is used to purify or separate certain compounds that are attached to particular molecules through reversible non-covalent bonds.
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
Molecular detail of spike Y453F
biochemical aspects of phenylketonuria disease
Purification of a new unknown protein that you isolated from tissue and
Assume that you have reached the following data during the characterization;
Gel filtration: Gel filtration in protein native conformation
When chromatographed, it has a molecular weight of 240000 daltons (240
kDa) is detected to be around.
Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride
subjected to gel filtration chromatography again under denatured conditions.
is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa)
a protein is obtained.
SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol
(Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis
being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons.
Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa)
is observed.
In the light of these findings, the quaternary/quaternary…
Chapter 11 Solutions
Biochemistry
Ch. 11 - Prob. 1PCh. 11 - Prob. 2PCh. 11 - Prob. 3PCh. 11 - Prob. 4PCh. 11 - Prob. 5PCh. 11 - Prob. 6PCh. 11 - Prob. 7PCh. 11 - Prob. 8PCh. 11 - Prob. 9PCh. 11 - Prob. 10P
Ch. 11 - Prob. 11PCh. 11 - Prob. 12PCh. 11 - Prob. 13PCh. 11 - Prob. 14PCh. 11 - Prob. 15PCh. 11 - Prob. 16PCh. 11 - Prob. 17PCh. 11 - Prob. 18PCh. 11 - Prob. 19PCh. 11 - Prob. 20PCh. 11 - Prob. 21PCh. 11 - Prob. 22PCh. 11 - Prob. 23PCh. 11 - Prob. 24PCh. 11 - Prob. 25PCh. 11 - Prob. 26PCh. 11 - Prob. 27PCh. 11 - Prob. 28PCh. 11 - Prob. 29PCh. 11 - Prob. 30PCh. 11 - Prob. 31PCh. 11 - Prob. 32PCh. 11 - Prob. 33PCh. 11 - Prob. 34PCh. 11 - Prob. 35PCh. 11 - Prob. 36PCh. 11 - Prob. 37PCh. 11 - Prob. 38PCh. 11 - Prob. 39P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Reposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?arrow_forwardActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1 Alanyl-phenylalanine 2. Lysyl-alanine 3.Phenylalanyl-tyrosyl-leucinearrow_forwardQuestion:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SGarrow_forward
- Exponential expansion? Compare the amount of information inherent in the genome, the proteome, and the glycome.arrow_forwardBIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : In human beings, what is the major control of de novo pyrimidine nucleotide synthesis? A. substrate availability B. competitive inhibition of carbamoyl phosphate synthetase II C. feedback inhibition of glutamine-PRPP amidotransferase D. vailability of N-acetyl glutamatearrow_forwardActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartatearrow_forward
- Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.arrow_forwarddisadvantage of using protein blastarrow_forwardThinking about the complexity of biochemical systems as they relate to the human body and the specificity of DNA, why can we not describe the “average” behavior of a DNA molecule?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning