Which glycoprotein binds with hemoglobin to facilitate removal by the reticuloendothelial system?

Unlock all questions

This demo includes only 20 questions. Upgrade to access hundreds of questions, flashcards, exam simulations, and disable ads.

Full question bankExam simulationsFlashcards
From $9.99Unlock all

Prepare for the Ciulla Clinical Chemistry Test with comprehensive flashcards and detailed multiple-choice questions. Each question includes helpful hints and explanations. Boost your confidence and excel in your test!

Multiple Choice

Which glycoprotein binds with hemoglobin to facilitate removal by the reticuloendothelial system?

Explanation:
Free hemoglobin released into the bloodstream is scavenged by a plasma glycoprotein called haptoglobin. It binds Hb with high affinity, forming a stable haptoglobin–hemoglobin complex. This complex is recognized and cleared by macrophages of the reticuloendothelial system (notably in the liver and spleen) via receptors such as CD163, preventing the toxic effects of free heme and conserving iron. The other proteins listed do not bind free hemoglobin in this way: ceruloplasmin carries copper and acts as a ferroxidase, alpha1-antitrypsin inhibits proteases, and fibrinogen is involved in clot formation.

Free hemoglobin released into the bloodstream is scavenged by a plasma glycoprotein called haptoglobin. It binds Hb with high affinity, forming a stable haptoglobin–hemoglobin complex. This complex is recognized and cleared by macrophages of the reticuloendothelial system (notably in the liver and spleen) via receptors such as CD163, preventing the toxic effects of free heme and conserving iron. The other proteins listed do not bind free hemoglobin in this way: ceruloplasmin carries copper and acts as a ferroxidase, alpha1-antitrypsin inhibits proteases, and fibrinogen is involved in clot formation.

More Multiple Choice Questions
Subscribe

Get the latest from Examzify

You can unsubscribe at any time. Read our privacy policy