Concept explainers
(a)
Interpretation:
The reason for a “smear” in lane 1 of the western blot gel should be explained.
Concept introduction:
Glycogenin is an enzyme which catalyzes the formation of short glycogen primers from glucose molecules.
Alpha amylase catalyzes the hydrolysis of alpha linkages in polysaccharides and release glucose and maltose.
SDS-PAGE is a biochemical technique used to separate charged molecules from a mixture, according to their molecular masses. SDS acts as a surfactant and negatively charge the proteins evenly. Thus, separating them only based on their molecular mass.
Western blot is visualizing technique which is commonly used for analyzing proteins. Proteins separated by SDS-PAGE electrophoresis is transferred to a membrane, so that it can be visualized easily with the specific antibodies against the target protein.
(b)
Interpretation:
The significance of the decrease in high molecular weight bands in lane 2 should be explained.
Concept introduction:
Glycogenin is an enzyme which catalyzes the formation of short glycogen primers from glucose molecules.
Alpha amylase catalyzes the hydrolysis of alpha linkages in polysaccharides and release glucose and maltose.
SDS-PAGE is a biochemical technique used to separate charged molecules from a mixture, according to their molecular masses. SDS acts as a surfactant and negatively charge the proteins evenly. Thus, separating them only the basis of their molecular mass.
Western blot is a visualizing technique which is commonly used for analyzing proteins. Proteins separated by SDS-PAGE electrophoresis are transferred to a membrane, so that it can be visualized easily with the specific antibodies against the target protein.
(c)
Interpretation:
Significance of the difference between lane 2 and 3 should be explained
Concept introduction:
Glycogenin is an enzyme which catalyzes the formation of short glycogen primers from glucose molecules.
Alpha amylase catalyzes the hydrolysis of alpha linkages in polysaccharides and release glucose and maltose.
SDS-PAGE is a biochemical technique used to separate charged molecules from a mixture, according to their molecular masses. SDS acts as a surfactant and negatively charge the proteins evenly. Thus, separating them only based on their molecular mass.
Western blot is a visualizing technique which is commonly used for analyzing proteins. Proteins separated by SDS-PAGE electrophoresis is transferred to a membrane, so that it can be visualized easily with the specific antibodies against the target protein.
(d)
Interpretation:
A plausible reason for no difference between lanes 3 and 4 should be suggested.
Concept introduction:
Glycogenin is an enzyme which catalyzes the formation of short glycogen primers from glucose molecules.
Alpha amylase catalyzes the hydrolysis of alpha linkages in polysaccharides and release glucose and maltose.
SDS-PAGE is a biochemical technique used to separate charged molecules from a mixture, according to their molecular masses. SDS acts as a surfactant and charges the proteins both negatively and evenly. Thus, separating them only based on their molecular mass.
Western blot is a visualizing technique which is commonly used for analyzing proteins. Proteins separated by SDS-PAGE electrophoresis are transferred to a membrane, so that it can be visualized easily with the specific antibodies against the target protein.
(e)
Interpretation:
The 66 kDabands observed in all the lanes treated with amylase, despite the fact that the cells were treated differently should be justified.
Concept introduction:
Glycogenin is an enzyme which catalyzes the formation of short glycogen primers from glucose molecules.
Alpha amylase catalyzes the hydrolysis of alpha linkages in polysaccharides and release glucose and maltose.
SDS-PAGE is a biochemical technique used to separate charged molecules from a mixture, according to their molecular masses. SDS acts as a surfactant and charges the proteins both negatively and evenly. Thus, separating them only based on their molecular mass.
Western blot is a visualizing technique which is commonly used for analyzing proteins. Proteins separated by SDS-PAGE electrophoresis are transferred to a membrane, so that it can be visualized easily with the specific antibodies against the target protein.
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Chapter 21 Solutions
BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
- Draw a typical axodendritic synapse, including a specific neurotransmitter of your choice, its associated postsynaptic receptors (indicating whether they are ionotropic or metabotropic), and any associated reuptake transporters or degradation enzymes. Please include a description of what specific steps would occur as an action potential reaches the axonal terminal.arrow_forwardGive a full arrow pushing mechanism of the spontaneous redox reaction between NAD+/NADH and oxaloacetate/malate. Please include diagram drawing of the mechanism! (Thank You!)arrow_forward18. Which one of the compounds below is the major organic product obtained from the following series of reactions? 1. BH3 2. H2O2, NaOH H₂CrO4 CH2N2 oro ororos A B C D Earrow_forward
- 17. Which one of the compounds below is the major organic product obtained from the following series of reactions? CI benzyl alcohol OH PBr3 Mg 1. CO2 SOCl2 ? ether 2. H+, H₂O CI Cl HO OH CI Cl A B C D Earrow_forward14. What is the IUPAC name of this compound? A) 6-hydroxy-4-oxohexanenitrile B) 5-cyano-3-oxo-1-pentanol C) 5-cyano-1-hydroxy-3-pentanone D) 1-cyano-5-hydroxy-3-pentanone E) 5-hydroxy-3-oxopentanenitrile HO. CNarrow_forward13. What is the IUPAC name of this compound? A) 5-hydroxy-3,3-dimethylpentanoic acid B) 3,3-dimethylpentanoic acid C) 3,3-dimethyl-1-oxo-1,5-pentanediol D) 1,5-dihydroxy-3,3-dimethylpentanal E) 4-hydroxy-2,2-dimethylbutanoic acid HO OHarrow_forward
- Help me understand how carbon disulfide leads to toxicity in the brain, using terms like distal axonopathy, neurofilaments, covalent cross-linking, adducts, etc.,...please intuitively explain what is happening and where and the effects of it. For example, I know that CS2 reacts with amide and sulfhydryl groups on proteins, but what proteins exactly and where are they located?arrow_forwardWhat is the standard free energy change (in kJ/mole) of the spontaneous reaction between Oxygen and NADH to form H2O2 and NAD+?arrow_forwardRedox Chemistry: Give standard free energy changes expected for the following reactions:-Succinate -> fumarate (using FAD/FADH2)-Oxaloacetate -> Malate (using NAD/NADH)-NADH --> NAD+ (using FMN/FMNH2)-CoQ --> CoQH2 (using Cytochrome C)arrow_forward
- Give examples of balanced redox reactions that match the following:-Catabolic-Anabolic-Oxidative-Reductivearrow_forwardIf there are 20uM of a GLUT2 transporter on the surface of a cell, each able to move 8 per second, and 50mM glucose outside of the cell, what is the flux into the cell in mM/sec?arrow_forwardA transporter is responsible for antiporting calcium and glucose. The transporter brings glucose into the cell and sends calcium out of the cell. If blood [calcium] = 2.55mM and intracellular [calcium] = 7uM, blood [glucose] = 5.2mM, and intracellular [glucose] = 40uM, what is the free energy of transport? Assume a membrane potential of 62mV (negative inside).arrow_forward
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