Videos
(a)
To tabulate: The values of specific activity, %yield, and fold purification for the crude extract, DEAE-cellulose chromatography, and affinity chromatography from the given values of protein concentration.
Concept introduction: DEAE (Diethylaminoethyl) cellulose chromatography is an ion exchange chromatography used for the separation and purification of proteins. DEAE cellulose is a weak anion exchanger, so the negatively charged protein binds to DEAE. It separates the substance based on its charges such that a negatively charged protein binds with the positively charged DEAE. Affinity chromatography is a separation method based on interactions. This is the efficient purification method for complex proteins and other complexes.
(b)
To determine: The step in which DEAE or affinity chromatography causes the greatest loss of myoglobin in the given table.
Concept introduction: DEAE (Diethylaminoethyl) cellulose chromatography is an ion exchange chromatography used for the separation and purification of proteins. DEAE cellulose is a weak anion exchanger, so the negatively charged protein binds to DEAE. It separates the substance based on their charges, where a negatively charged protein binds with the positively charged DEAE. Affinity chromatography is a separation method based on the interactions. This is the efficient purification method for complex proteins and other complexes.
(c)
To explain: The step in which DEAE or affinity chromatography causes greater purification is given in the table.
Concept introduction: DEAE (Diethylaminoethyl) cellulose chromatography is an ion exchange chromatography used for the separation and purification of proteins. DEAE cellulose is a weak anion exchanger, so the negatively charged protein binds to DEAE. It separates the substance based on its charges where a negatively charged protein binds with the positively charged DEAE. Affinity chromatography is a separation method based on interactions. This is the efficient purification method for complex proteins and other complexes.
(d)
To explain: The best step that could use for the purification of myoglobin.
Concept introduction: DEAE (Diethylaminoethyl) cellulose chromatography is an ion exchange chromatography used for the separation and purification of proteins. DEAE cellulose is a weak anion exchanger, so the negatively charged protein binds to DEAE. It separates the substance based on its charges, where a negatively charged protein binds with the positively charged DEAE. Affinity chromatography is a separation method based on interactions. This is the efficient purification method for complex proteins and other complexes.
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Chapter 5 Solutions
FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
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- Below is a fractional saturation curve for O2 binding to adult hemoglobin. Assume that curve Y represents a system at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve Z represents a system that ___________________ Curve Z: is at pH 7.4 with a higher than normal physiological level of 2,3-BPG. is at pH 7.4 with a normal physiological level of 2,3-BPG but with a decreased level of CO2. has a higher pH with a normal physiological level of 2,3-BPG. has a higher pH with a lower than physiological level of 2,3-BPG.arrow_forwardWhich is a homotropic positive effector of aspartate transcarbamoylase (ATCase)? oxygen CTP aspartate ATParrow_forwardThe reaction scheme shows the mechanism of chymotrypsin-catalyzed peptide hydrolysis. Select ALL CORRECT statements regarding the chymotrypsin mechanism. Serine is the nucleophile in the step 3. Histidine is a general base in the step 2. Carbonyl carbon is the electrophile in the step 3. Histidine is a general acid in the step 4. Carbonyl carbon is the nucleophile in the step 3. This is an example of covalent catalysis. Aspartate is the electrophile in the step 3. Histidine is the nucleophile in the step 3.arrow_forward
- The following shows a protein with mostly beta sheet secondary structures. Which force stabilizes the beta sheet secondary structure of proteins? hydrophobic interactions between nonpolar amino acid side chains within the protein. electrostatic interactions between lysine and aspartic acid residues within the protein. hydrogen bonding between hydrogen bond donors and hydrogen bond acceptors of the peptide backbone. covalent disulfide linkages between cysteine residues within the protein.arrow_forwardThe Lineweaver-Burk plot was obtained when enzyme inhibition study was done in the absence and presence of 0.50 mM inhibitor. Answer the following questions using correct units and significant figures: (a) What is the mode of inhibition, competitive, uncompetitive, mixed, or noncompetitive? Explain your answer. (b) What can you say about the finding site for the inhibitor in relation to the active site of the enzyme? Explain your answer. (c) Calculate the Km and Vmax in the absence of inhibitor. (d) Calculate the Km and Vmax in the presence of 0.50 mM inhibitor. (e) Calculate the KI of the inhibitor using the given equations for reversible inhibition. Which has a higher affinity, the substrate or the inhibitor? How can you tell?arrow_forwardWhich peptide sequence is most likely to be found in the interior portion of a water-soluble globular protein? GGDGEMG DSKSTEG GAIVLWL IVAKSLIarrow_forward
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