Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

6. Enzymes and Enzyme Kinetics

Enzymes

Biochemistry

6. Enzymes and Enzyme Kinetics

Enzymes

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Multiple Choice

The enzyme pepsin is formed from pepsinogen through the action of:

trypsin

bile salts

hydrochloric acid (HCl)

amylase

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Verified step by step guidance

Understand the context: Pepsin is a digestive enzyme that breaks down proteins in the stomach. It is initially produced in an inactive form called pepsinogen to prevent damage to the stomach lining.

Recognize the activation mechanism: Pepsinogen is converted into its active form, pepsin, through the action of hydrochloric acid (HCl) in the stomach. HCl lowers the pH, creating an acidic environment necessary for this conversion.

Clarify why other options are incorrect: Trypsin is involved in protein digestion in the small intestine, not the stomach. Bile salts aid in fat digestion, and amylase breaks down carbohydrates. None of these are involved in activating pepsinogen.

Relate the process to physiological conditions: The stomach's acidic pH (around 1.5-3.5) is maintained by HCl, which not only activates pepsinogen but also helps denature proteins for easier digestion.

Summarize the key concept: The activation of pepsinogen into pepsin is a crucial step in protein digestion and is specifically triggered by hydrochloric acid (HCl) in the stomach.