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Which enzyme was conjugated to the LDL cholesterol complex to detect the presence of cholesterol intake by the cell?

A. Lipase
B. Catalase
C. Horseradish Peroxidase (HRP)
D. Amylase

User Johannes
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1 Answer

5 votes

Final answer:

The enzyme conjugated to the LDL cholesterol complex to detect cholesterol intake by cells is Horseradish Peroxidase (HRP), used due to its enzymatic activity in biological detection assays. On the other hand, caseinase is classified as an extracellular protease that breaks down proteins outside of cells.

Step-by-step explanation:

To detect cholesterol intake by a cell using the receptor-mediated endocytosis of low-density lipoprotein (LDL), it is common to use an enzyme conjugated to LDL. This allows the complex to be visualized during experimental techniques. The enzyme typically used for this conjugation is Horseradish Peroxidase (HRP), which would make option C the correct answer for the detection of cholesterol intake by the cell.

Additional Information

HRP is often used in biological assays because of its ability to catalyze the oxidation of the substrate in the presence of hydrogen peroxide, producing a detectable change that is used as a marker for the presence of the LDL cholesterol complex.

In comparison, the other enzymes listed serve different functions: Lipase (option B) is involved in the hydrolysis of fats, Catalase (option B) catalyzes the decomposition of hydrogen peroxide to water and oxygen, and Amylase (option D) is involved in breaking down carbohydrates.

Regarding Caseinase

Caseinase is a type of extracellular protease (option C), which means it is involved in the breakdown of proteins outside the cell. Proteases like caseinase are crucial for various biological processes, including degradation of dietary proteins.

User Husqvik
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