Campbell Biology, Books a la Carte Edition (11th Edition)
11th Edition
ISBN: 9780134154121
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece
Publisher: PEARSON
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Chapter 8.4, Problem 4CC
Summary Introduction
To draw: A graph depicting the
Introduction: Lysosomes are the enzymes that are present in the cytoplasm and are used in breaking down of molecules such as carbohydrates. It also digests foreign agents during phagocytosis mechanism in many cellular organisms. It is also released during apoptotic reactions.
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Chapter 8 Solutions
Campbell Biology, Books a la Carte Edition (11th Edition)
Ch. 8.1 - MAKE CONNECTIONS How does the second law of...Ch. 8.1 - Describe the forms of energy found in an apple as...Ch. 8.1 - WHAT IF? If you place a teaspoon of sugar in the...Ch. 8.2 - Cellular respiration uses glucose and oxygen,...Ch. 8.2 - VISUAL SKILLS How would the processes of...Ch. 8.2 - WHAT IF? Some nighttime partygoers wear glow-in-...Ch. 8.3 - How does ATP typically transfer energy from an...Ch. 8.3 - Prob. 2CCCh. 8.3 - MAKE CONNECTIONS Does Figure 8.11a show passive...Ch. 8.4 - Many spontaneous reactions occur very slowly. Why...
Ch. 8.4 - Prob. 2CCCh. 8.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 8.4 - Prob. 4CCCh. 8.5 - How do an activator and an inhibitor have...Ch. 8.5 - Prob. 2CCCh. 8 - Explain how the highly ordered structure of a cell...Ch. 8 - Explain the meaning of each component in the...Ch. 8 - Describe the ATP cycle: How is ATP used and...Ch. 8 - How do both activation energy barriers and enzymes...Ch. 8 - Prob. 8.5CRCh. 8 - Choose the pair of terms that correctly completes...Ch. 8 - Prob. 2TYUCh. 8 - Which of the following metabolic processes can...Ch. 8 - Prob. 4TYUCh. 8 - Some bacteria art metabolically active in hot...Ch. 8 - If an enzyme is added to a solution where its...Ch. 8 - Prob. 7TYUCh. 8 - EVOLUTION CONNECTION Some people argue that...Ch. 8 - Prob. 9TYUCh. 8 - WRITE ABOUT A THEME: ENERGY AND MATTER Life...Ch. 8 - Prob. 11TYU
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- How many copies of a protein need to be present in a cell in order for it to be visible as a band on an SDS gel? Assume that you can load 100 µg of cell extract onto a gel and that you can detect 10 ng in a single band by sil ver staining the gel. The concentration of protein in cells is about 200 mg/mL, and a typical mammalian cell has a volume of about 1000 μm³ and a typical bacterium a vol ume of about 1 µm³. Given these parameters, calculate the number of copies of a 120-kd protein that would need to be present in a mammalian cell and in a bacterium in order to give a detectable band on a gel. You might try an order-of-magnitude guess before you make the calcula tions.arrow_forwardHere is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylatedarrow_forwardPlasmolysis in plant cell Describe the cell in 0.1 % Salt Solution and explain the process. Describe the cell in 5 % Salt Solution and explain the process.arrow_forward
- A transmembrane protein helps catalyze the transport of solute A from the INSIDE TO the OUTSIDE of a cell. The reaction can be represented by the reaction coordinate diagram below. It is possible to conclude that the concentration of A on the outside of the cell is than its concentration on the inside AND that it is_ to expect that the protein will at some point form a continuous path between th cytosol and the extracellular environment. A inside A outside reaction coordinate O lower; reasonable O higher; unreasonable O higher; reasonable free energyarrow_forwardHow many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.arrow_forwardIn order to investigate the action of a bacterial membrane protein that is a light-driven proton pump, you purify the protein and assemble it together with phospholipids into liposomes that contain an indicator dye, which is blue at high pH, colorless at neutral pH, and red at low pH. You then expose the liposomes, in an aqueous solution, to sunlight. The interior of the liposomes turn blue. Further investigatin of the proton pump protein you find that treatment of either intact bacteria or the purified protein with the protease chymotrypsin result in cleavage of the protein at a single site near the amino terminus, which destroys its capacity to pump protons. When you treat the liposomes described above with chymotrypsin, the interior of the liposomes remains colorless. Create an illustration/ diagram of that illustrates the orientation of the pump protein in the plasma membrane of the intact bacterium and the direction in which it pumps protons.arrow_forward
- In order to investigate the action of a bacterial membrane protein that is a light-driven proton pump, you purify the protein and assemble it together with phospholipids into liposomes that contain an indicator dye, which is blue at high pH, colorless at neutral pH, and red at low pH. You then expose the liposomes, in an aqueous solution, to sunlight. The interior of the liposomes turn blue. Further investigatin of the proton pump protein you find that treatment of either intact bacteria or the purified protein with the protease chymotrypsin result in cleavage of the protein at a single site near the amino terminus, which destroys its capacity to pump protons. When you treat the liposomes described above with chymotrypsin, the interior of the liposomes remains colorless. From these results create a diagram of that illustrates the orientation of the pump protein in the plasma membrane of the intact bacterium and the direction in which it pumps protons. Explain your reasoning.arrow_forwardIn the early days of ribosome research, before the exact role of ribosomes was clear, a researcher made the following observation. She could find, in sedimentation experiments on bacterial lysates, not only 3OS, 50S, and 70S particles, but also some particles that sedimented at about 100S and 130S. When she treated such a mixture with EDTA, everything dissociated to 30S and 50S particles. Upon adding divalent ions, she could regain 70S particles, but never 100S or 130S particles. (a) Suggest what the 10oS and 130S particles might represent, in light of cur- rent knowledge of protein synthesis. What important discovery did the researcher miss? (b) Why do you think reassociation to 100S and 130S particles did not work?arrow_forwardMatch the letter in the diagram with the accumulation or localization of active or about to be active protein in a given cellular contacts which is wild type unless specified. 1. Plasma membrane v-snare 2. Endosomal v-snare 3. Dynamin 4. A protein with n-sig only in a class e yeast mutant Match with A, B, C, D on diagramarrow_forward
- please help with both questionsarrow_forward. In the early days of ribosome research, before the exact role of ribo- somes was clear, a researcher made the following observation. She could find, in sedimentation experiments on bacterial lysates, not only 30S, 50S, and 70S particles but also some particles that sedi- mented at about 100S and 130S. When she treated such a mixture with EDTA, everything dissociated to 30S and 50S particles. Upon adding divalent ions, she could regain 70S particles, but never 100S or 130S particles. (a) Suggest what the 100S and 130S particles might represent, in light of current knowledge of protein synthesis. What important dis- covery did the researcher miss? (b) Why do you think reassociation to 100S and 130S particles did not work?arrow_forwardThe dimensions of prokaryotic ribosomes are approximately 14 nm by 20 nm. If ribosomes occupy 20% of the volume of a bacterial cell, calculate how many ribosomes are in a typical cell as E. coli. Assume that the shape of a ribosome is approximately that of a cylinder.arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY