Search results
Results from the WOW.Com Content Network
The physiological importance of peroxiredoxins is indicated by their relative abundance (one of the most abundant proteins in erythrocytes after hemoglobin is peroxiredoxin 2). Their function is the reduction of peroxides, specifically hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite.
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—via ...
4.7 to 6.1 million (male), 4.2 to 5.4 million (female) erythrocytes: [13] Red blood cells contain the blood's hemoglobin and distribute oxygen. Mature red blood cells lack a nucleus and organelles in mammals. The red blood cells (together with endothelial vessel cells and other cells) are also marked by glycoproteins that define the different ...
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.
It does not identify the Rh(D) antigen (Rh blood type). The bedside card method of blood grouping relies on visual agglutination to determine an individual's blood group. The card contains dried blood group antibody reagents fixed onto its surface. A drop of the individual's blood is placed on each blood group area on the card.
Erythropoietin (/ ɪ ˌ r ɪ θ r oʊ ˈ p ɔɪ. ɪ t ɪ n,-r ə-,-p ɔɪ ˈ ɛ t ɪ n,-ˈ iː t ɪ n /; [1] [2] [3] EPO), also known as erythropoetin, haematopoietin, or haemopoietin, is a glycoprotein cytokine secreted mainly by the kidneys in response to cellular hypoxia; it stimulates red blood cell production (erythropoiesis) in the bone marrow.
Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening. Nitric oxide is capable of converting a small fraction of hemoglobin to methemoglobin in red blood cells. The latter reaction is a remnant activity of the more ancient nitric oxide dioxygenase function of globins.
They are produced in the liver and contain binding sites for two Fe 3+ ions. [6] Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein. [7] [8] Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool ...