Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th
Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th
7th Edition
ISBN: 9781305081086
Author: STOKER, H. Stephen
Publisher: Brooks Cole
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Chapter 26, Problem 26.102EP

(a)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin in whose production “ring-opening” occurs.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center. The structure of the heme group is:

Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th, Chapter 26, Problem 26.102EP , additional homework tip  1

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

(b)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin in whose production a carbon-carbon double bond is changed to a carbon-carbon single bond.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center.

The structure of the heme group is:

Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th, Chapter 26, Problem 26.102EP , additional homework tip  2

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

(c)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin that is rendered more water soluble by use of a glucose derivative.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center.

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

The structure of the heme group is:

Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th, Chapter 26, Problem 26.102EP , additional homework tip  3

(d)

Interpretation Introduction

Interpretation: To identify the heme degradation product (1) bilirubin, (2) biliverdin, (3) stercobilin, and (4) urobilin which is bile pigment and has a yellowish color.

Concept introduction: Hemoglobin is a heme protein present in the red blood cells. The protein part is called globin and the non-protein part is heme. Heme is the prosthetic group that contains 4 pyrrole groups bonded together and has an iron atom in the center.

The structure of the heme group is:

Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th, Chapter 26, Problem 26.102EP , additional homework tip  4

The first step of degradation of heme involves opening of pyrrole ring with the release of the iron atom and production of biliverdin. The iron atom released becomes part of ferritin protein. Biliverdin produced is converted bilirubin in the spleen. Bilirubin is then transported to the liver where attachment of sugar residues to the propionate side chains of the bilirubin occurs to make it more soluble. Then more solubilized bilirubin is excreted in bile and finally to the small intestine. In the small intestine, it is converted into stercobilin for excretion in feces or urobilin for excretion in urine.

Bile pigments are the colored degradation product of tetrapyrrole carbon arrangement of heme portion of hemoglobin. These are excreted in bile and give characteristic color to urine and feces.

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Chapter 26 Solutions

Study Guide with Selected Solutions for Stoker's General, Organic, and Biological Chemistry, 7th

Ch. 26.3 - Prob. 4QQCh. 26.3 - Prob. 5QQCh. 26.3 - Most aminotransferases are specific for the keto...Ch. 26.4 - Which of the following statements concerning the...Ch. 26.4 - Prob. 2QQCh. 26.4 - The two fuels for the urea cycle are a. carbamoyl...Ch. 26.4 - Prob. 4QQCh. 26.4 - Prob. 5QQCh. 26.4 - Prob. 6QQCh. 26.5 - Which of the following statements concerning the...Ch. 26.5 - Prob. 2QQCh. 26.5 - Prob. 3QQCh. 26.5 - Prob. 4QQCh. 26.6 - Prob. 1QQCh. 26.6 - How many of the standard amino acids are...Ch. 26.6 - The simplest pathways for amino acid biosynthesis...Ch. 26.7 - Prob. 1QQCh. 26.7 - Which of the following statements concerning the...Ch. 26.7 - Prob. 3QQCh. 26.7 - In the degradation of heme, the iron atom present...Ch. 26.8 - In degradation of the sulfur-containing amino acid...Ch. 26.8 - Prob. 2QQCh. 26.8 - Prob. 3QQCh. 26.8 - Prob. 4QQCh. 26.9 - Prob. 1QQCh. 26.9 - Prob. 2QQCh. 26.9 - Prob. 3QQCh. 26.10 - Prob. 1QQCh. 26.10 - Prob. 2QQCh. 26.10 - Prob. 3QQCh. 26 - Prob. 26.1EPCh. 26 - Indicate whether each of the following aspects of...Ch. 26 - Indicate whether each of the following pairings of...Ch. 26 - Indicate whether each of the following pairings of...Ch. 26 - Indicate whether each of the following statements...Ch. 26 - Prob. 26.6EPCh. 26 - Prob. 26.7EPCh. 26 - Prob. 26.8EPCh. 26 - Prob. 26.9EPCh. 26 - Prob. 26.10EPCh. 26 - Prob. 26.11EPCh. 26 - Prob. 26.12EPCh. 26 - Prob. 26.13EPCh. 26 - Prob. 26.14EPCh. 26 - Indicate whether each of the following situations...Ch. 26 - Indicate whether each of the following situations...Ch. 26 - Prob. 26.17EPCh. 26 - Prob. 26.18EPCh. 26 - Prob. 26.19EPCh. 26 - Prob. 26.20EPCh. 26 - Prob. 26.21EPCh. 26 - Prob. 26.22EPCh. 26 - Prob. 26.23EPCh. 26 - Prob. 26.24EPCh. 26 - Prob. 26.25EPCh. 26 - Prob. 26.26EPCh. 26 - Prob. 26.27EPCh. 26 - Prob. 26.28EPCh. 26 - Prob. 26.29EPCh. 26 - Prob. 26.30EPCh. 26 - Prob. 26.31EPCh. 26 - Prob. 26.32EPCh. 26 - Prob. 26.33EPCh. 26 - Prob. 26.34EPCh. 26 - Prob. 26.35EPCh. 26 - Prob. 26.36EPCh. 26 - Prob. 26.37EPCh. 26 - Prob. 26.38EPCh. 26 - Prob. 26.39EPCh. 26 - Prob. 26.40EPCh. 26 - Prob. 26.41EPCh. 26 - Prob. 26.42EPCh. 26 - Prob. 26.43EPCh. 26 - Draw the structure of the -keto acid produced from...Ch. 26 - Prob. 26.45EPCh. 26 - Prob. 26.46EPCh. 26 - Prob. 26.47EPCh. 26 - Prob. 26.48EPCh. 26 - Prob. 26.49EPCh. 26 - Prob. 26.50EPCh. 26 - Prob. 26.51EPCh. 26 - Prob. 26.52EPCh. 26 - Prob. 26.53EPCh. 26 - Prob. 26.54EPCh. 26 - Prob. 26.55EPCh. 26 - Prob. 26.56EPCh. 26 - Prob. 26.57EPCh. 26 - Prob. 26.58EPCh. 26 - Prob. 26.59EPCh. 26 - Prob. 26.60EPCh. 26 - Prob. 26.61EPCh. 26 - Prob. 26.62EPCh. 26 - Prob. 26.63EPCh. 26 - Prob. 26.64EPCh. 26 - Prob. 26.65EPCh. 26 - Prob. 26.66EPCh. 26 - Prob. 26.67EPCh. 26 - Prob. 26.68EPCh. 26 - Prob. 26.69EPCh. 26 - Prob. 26.70EPCh. 26 - Prob. 26.71EPCh. 26 - Prob. 26.72EPCh. 26 - Prob. 26.73EPCh. 26 - Prob. 26.74EPCh. 26 - Prob. 26.75EPCh. 26 - Prob. 26.76EPCh. 26 - Prob. 26.77EPCh. 26 - Prob. 26.78EPCh. 26 - Prob. 26.79EPCh. 26 - Prob. 26.80EPCh. 26 - Prob. 26.81EPCh. 26 - Prob. 26.82EPCh. 26 - Prob. 26.83EPCh. 26 - Prob. 26.84EPCh. 26 - Prob. 26.85EPCh. 26 - Prob. 26.86EPCh. 26 - Prob. 26.87EPCh. 26 - Prob. 26.88EPCh. 26 - Prob. 26.89EPCh. 26 - Prob. 26.90EPCh. 26 - Prob. 26.91EPCh. 26 - Prob. 26.92EPCh. 26 - Prob. 26.93EPCh. 26 - Prob. 26.94EPCh. 26 - Prob. 26.95EPCh. 26 - Prob. 26.96EPCh. 26 - Prob. 26.97EPCh. 26 - Which bile pigment is responsible for the...Ch. 26 - Prob. 26.99EPCh. 26 - Prob. 26.100EPCh. 26 - Prob. 26.101EPCh. 26 - Prob. 26.102EPCh. 26 - Prob. 26.103EPCh. 26 - Prob. 26.104EPCh. 26 - Prob. 26.105EPCh. 26 - Prob. 26.106EPCh. 26 - Prob. 26.107EPCh. 26 - Prob. 26.108EPCh. 26 - Prob. 26.109EPCh. 26 - Prob. 26.110EPCh. 26 - Prob. 26.111EPCh. 26 - Prob. 26.112EPCh. 26 - Prob. 26.113EPCh. 26 - Prob. 26.114EPCh. 26 - Prob. 26.115EPCh. 26 - Prob. 26.116EP
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