2 Angiotensin Converting Enzyme (ACE) is the target of ACE inhibitors such ascaptopril that are used therapeutically to control blood pressure. The enzymeACE converts angiotensin I to angiotensin II. Angiotensin II is an octapeptidewith the sequence Asp-Arg-Val-Tyr-Ile-His-Pro-Phe. What will its net chargebe at pH 7?OA) -2B) -1OcoOD)D) +OE) +2 A competitive inhibitor diminishes the rate of catalysis:A)By reducing the proportion of enzyme molecules bound to asubstrate.B) By altering the shape of the active site of the enzymeOC) By binding to a regulatory subunitOD) By enhancing the interaction between enzyme and reaction product

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Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter9: Parenteral Medication Labels And Dosage Calculation

Section: Chapter Questions

Problem 6.7P

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Angiotensin Converting Enzyme (ACE) is the target of ACE inhibitors such as captopril that are used therapeutically to control blood pressure. The enzyme ACE converts angiotensin I to angiotensin II. Angiotensin II is an octapeptide with the sequence Asp-Arg-Val-Tyr-Ile-His-Pro-Phe. What will its net charge be at pH 7? A) -2 B) -1 O C) O D) +1 E) +2
Amino acid analysis of the peptide angiotensin II shows the presence of eight different aminoacids in equimolar amounts: Arg, Asp, His, Ile, Phe, Pro, Tyr and Val. Partial hydrolysis ofangiostensin II with dilute HCl yields the following fragmentsa.) Asp –Arg- Val –Tyr b.) Ile –his –Proc.) Pro –Phe d.) Val – tyr – Ile –His a.)What is the sequence of angiostensin II and what Fragment would result if angiotensin II were cleaved with trypsin? Withchymotrypsin?
An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?
A decapeptide was isolated from a thermophilic bacteria. Treatment of this peptide with 2- mercaptoethanol gave 2 pentapeptides. Further analysis of this peptide gave the following data: Trypsin: (M,Y), (K,Y,M), (K, 2A, 2C) Chymotrypsin: (2K, 2A, 2C, Y), (M), (Y,M) What is the primary structure of the decapeptide? Thank you.
If a protein lysate obtained is 1003 ug/ml What would be the total concentration of each lysate that is loaded into their well if you load just 25 ul of each?
You have an aqueous solution of hemoglobin (pl = 6.8) at pH 5.2, and currently the proteins are soluble. If you had 1M HCl and 1M NaOH at your disposal, what could you do to precipitate the albumin out of solution? add NaOH to the solution O add HCl to the solution O add NaOH to the solution, then add equal volume of HCl to the solution O add HCl to the solution, then add equal volume of NaOH to the solution
You have an aqueous solution of hemoglobin (pl = 6.8) at pH 6.5, and currently the proteins are soluble. If you had 1 M HCl and 1M NaOH at your disposal, what could you do to precipitate the albumin out of solution? O add NaOH to the solution add HCl to the solution add NaOH to the solution, then add equal volume of HCl to the solution O add HCl to the solution, then add equal volume of NaOH to the solution An error has been detected in your answer. Check for typos, miscalculations etc. before submitting your answer. Submit Answer Try Another Version 1 item attempt remaining
Which structure represents d-erythrose?
A mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2 ? v First 1. Alanine v Second 2. Glutamic Acid v Third 3. Glycine v Fourth 4. Lysine v Fifth 5. Threonine 6. No separation
Can you please help me how to draw tripeptide ile-leu-arg and indicate the torsion angles phi and psi for leucine?
After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
A mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by anion exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2 ? v First 1. Alanine v Second 2. Glutamic Acid v Third 3. Glycine 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation

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