Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 16, Problem 19RE
RECALL Define the term reducing sugar.
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Please analze the gel electrophoresis column of the VRK1 kinase (MW: 39.71 kDa).
Lane 1: buffer
Lane 2 : Ladder
Lane 3: Lysate
Lane 4: Flowthrough
Lane 5: Wash
Lanes 6-8: E1, E2, E3
Lane 9: Dialyzed VRK1
Lane 10: LDH
Please help
You have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD.
Describe the architecture of the polypeptide component of this enzyme.
Chapter 16 Solutions
Biochemistry
Ch. 16 - RECALL Define the following terms: polysaccharide,...Ch. 16 - RECALL Name which, if any, of the following are...Ch. 16 - RECALL Name which, if any, of the following groups...Ch. 16 - RECALL What is the difference between an...Ch. 16 - RECALL How many possible epimers of D-glucose...Ch. 16 - RECALL Why are furanoses and pyranoses the most...Ch. 16 - RECALL How many chiral centers are there in the...Ch. 16 - REFLECT AND APPLY Following are Fischer...Ch. 16 - REFLECT AND APPLY The sugar alcohol often used in...Ch. 16 - REFLECT AND APPLY Consider the structures of...
Ch. 16 - REFLECT AND APPLY Two sugars are epimers of each...Ch. 16 - REFLECT AND APPLY How does the cyclization of...Ch. 16 - REFLECT AND APPLY Convert the following Haworth...Ch. 16 - REFLECT AND APPLY Convert each of the following...Ch. 16 - REFLECT AND APPLY Starting with a Fischer...Ch. 16 - REFLECT AND APPLY Starting with the open-chain...Ch. 16 - RECALL What is unusual about the structure of...Ch. 16 - RECALL What is the chemical difference between a...Ch. 16 - RECALL Define the term reducing sugar.Ch. 16 - BIOCHEMICAL CONNECTIONS What are the structural...Ch. 16 - RECALL Name two differences between sucrose and...Ch. 16 - REFLECT AND APPLY Draw a Haworth projection for...Ch. 16 - BIOCHEMICAL CONNECTIONS What is the metabolic...Ch. 16 - REFLECT AND APPLY Draw Haworth projection formulas...Ch. 16 - BIOCHEMICAL CONNECTIONS A friend asks you why some...Ch. 16 - RECALL What are some of the main differences...Ch. 16 - RECALL How does chitin differ from cellulose in...Ch. 16 - RECALL How does glycogen differ from starch in...Ch. 16 - RECALL What is the main structural difference...Ch. 16 - RECALL What is the main structural difference...Ch. 16 - RECALL How do the cell walls of bacteria differ...Ch. 16 - REFLECT AND APPLY Pectin, which occurs in plant...Ch. 16 - REFLECT AND APPLY Advertisements for a food...Ch. 16 - REFLECT AND APPLY Explain how the minor structural...Ch. 16 - REFLECT AND APPLY All naturally occurring...Ch. 16 - REFLECT AND APPLY An amylose chain is 5000 glucose...Ch. 16 - REFLECT AND APPLY Suppose that a polymer of...Ch. 16 - REFLECT AND APPLY Glycogen is highly branched....Ch. 16 - REFLECT AND APPLY No animal can digest cellulose....Ch. 16 - REFLECT AND APPLY How does the presence of -bonds...Ch. 16 - REFLECT AND APPLY How do the sites of cleavage of...Ch. 16 - BIOCHEMICAL CONNECTIONS What is the benefit of...Ch. 16 - REFLECT AND APPLY How would you expect the active...Ch. 16 - REFLECT AND APPLY Would you expect cross-linking...Ch. 16 - REFLECT AND APPLY Compare the information in the...Ch. 16 - REFLECT AND APPLY Why is it advantageous that...Ch. 16 - REFLECT AND APPLY Why is the polysaccharide chitin...Ch. 16 - REFLECT AND APPLY Could bacterial cell walls...Ch. 16 - REFLECT AND APPLY Some athletes eat diets high in...Ch. 16 - Prob. 50RECh. 16 - REFLECT AND APPLY Blood samples for research or...Ch. 16 - REFLECT AND APPLY Based on what you know about...Ch. 16 - RECALL What are glycoproteins? What are some of...Ch. 16 - BIOCHEMICAL CONNECTIONS Briefly indicate the role...
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- In a cell free preparation of beta-lactamase, penicillin is hydrolyzed in a D2O enriched assay. After one round of catalysis, where would you anticipate finding Deuterium? please help thank youarrow_forwardTo map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. question: the b-lactamase hydrolyzes the lactam-ring in antibiotics like penicillin. Describe the mechanism, of hydrolysis, insuring to include the involvement of S, D, and K in the reaction sequence. Please help!arrow_forwardThree of these amino acids participate in the proteolytic hydrolysis of polypeptides. Show the charge-relay network generated by the serine proteases and identify the nucleophilic species that initiates the hydrolysis. please help!arrow_forward
- You have isolated a protein and determined that the native molecular weight of the holoenzyme is 160 kD using size exclusion chromatography. Analysis of this protein using SDS-PAGE revealed 2 bands, one at 100 kD and one at 30 kD. 1. Describe the architecture of the polypeptide component of this enzyme. 2. The enzyme was found to be 0.829% NAD (by weight). What further can be said regarding the architecture? can you please help me with question number 2arrow_forwardTo map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Question: although S, K, and D are involved in the catalysis, the E in this hexapeptide does not participate in the hydrolysis of the b-lactam ring. Why is that?arrow_forwardTo map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. a) Using the experimental results described below deduce the primary sequence of the active site hexapeptide. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. please help!arrow_forward
- The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please helparrow_forwardTo map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?arrow_forwardTo map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!arrow_forward
- Which type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.arrow_forward+NH+ CO₂ +P H₂N + ATP H₂N NH₂ +ADParrow_forwardWhich type of enzyme catalyses the following reaction? oxidoreductase, transferase, hydrolase, lyase, isomerase, or ligase.arrow_forward
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