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Red blood cells (RBCs), referred to as erythrocytes (from Ancient Greek erythros ' red ' and kytos ' hollow vessel ', with -cyte translated as 'cell' in modern usage) in academia and medical publishing, also known as red cells, [1] erythroid cells, and rarely haematids, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen (O 2) to the body tissues ...
A glycophorin is a sialoglycoprotein of the membrane of a red blood cell.It is a membrane-spanning protein and carries sugar molecules. It is heavily glycosylated (60%). Glycophorins are rich in sialic acid, which gives the red blood cells a very hydrophilic-charged
Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Protein 4.1 (80 kD) interacts with spectrin and short actin filaments to form the
Hemoglobin is an iron-containing protein that gives red blood cells their color and facilitates transportation of oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs to be exhaled. [3] Red blood cells are the most abundant cell in the blood, accounting for about 40–45% of its volume.
Serum also does not contain all the formed elements of blood, which include blood cells, white blood cells (leukocytes, lymphocytes), red blood cells (erythrocytes), and platelets. [citation needed] The study of serum is serology. Serum is used in numerous diagnostic tests as well as blood typing.
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A:Normal red blood cells are shown flowing freely in a blood vessel on the top of the diagram. The inset image shows a cross-section of a normal red blood cell with normal hemoglobin. B:Demonstrates abnormal, sickled red blood cells blocking blood flow in a blood vessel (vaso-occlusive crisis). The inset image shows a cross-section of a sickle ...
These 24 repeats contain 3 structurally distinct binding sites ranging from repeat 1-14. These binding sites are quasi-independent of each other and can be used in combination. The interactions the sites use to bind to membrane proteins are non-specific and consist of: hydrogen bonding, hydrophobic interactions and electrostatic interactions.