Final answer:
Antibodies are not identical but are unique proteins that are highly specific, each binding to only one type of antigen. They play a crucial role in the immune response by targeting foreign cells or substances for destruction. The statement is false because antibodies are diverse and specialized, not identical.
Step-by-step explanation:
The statement that antibodies are identical large proteins in the blood that are effective in destroying multiple types of invading foreign particles is false. While it is true that antibodies are large, Y-shaped proteins that play a crucial role in the immune response, they are not identical. Antibodies have unique molecular structures, each designed to match and bind with only one specific type of antigen. An antigen could be a protein, carbohydrate, glycoprotein, or glycolipid on the surface of invading pathogens or foreign substances. When antibodies bind to their respective antigens, they signal the immune system to target these cells or substances for destruction, often via mechanisms such as phagocytosis or activation of the complement cascade.
Additionally, antibodies are also vital in the humoral immune response and can be transferred from one individual to another, conferring temporary protection against diseases—this is known as passive immunity. Depending on their class, antibodies can work by neutralizing pathogens or tagging them for destruction by other immune cells. With millions of different antibodies in our system, each is capable of targeting a specific pathogen, making the immune system highly specific and efficient.