Enzyme trypsinogen is changed to trypsin by

Options

A. Gastrin
B. Enterogastrone
C. Enterokinase
D. Secretin

Answer

To solve the question "Enzyme trypsinogen is changed to trypsin by," we can follow these steps:

### Step 1: Understand the context
- Trypsinogen is an inactive precursor (zymogen) of the enzyme trypsin, which is involved in protein digestion.

### Step 2: Identify the activation process
- In the digestive system, certain enzymes are secreted in an inactive form to prevent them from digesting the tissues that produce them. Trypsinogen is one such enzyme.

### Step 3: Locate the site of activation
- Trypsinogen is activated in the small intestine, specifically in the duodenum, where it is converted into trypsin.

### Step 4: Identify the enzyme responsible for activation
- The conversion of trypsinogen to trypsin is facilitated by another enzyme. The options provided are gastrin, enterogastron, enterokinase, and secretin.

### Step 5: Determine the correct answer
- Among the options, enterokinase (also known as enteropeptidase) is the enzyme that activates trypsinogen into trypsin. It is secreted by the cells of the duodenum and acts on trypsinogen to convert it into its active form, trypsin.

### Final Answer
- The enzyme trypsinogen is changed to trypsin by enterokinase.

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