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The form discussed here is the one found in the 1950s to be linked to Rh blood group and more recently shown to be caused by a defect in protein 4.1. 'Rh-unlinked' forms of elliptocytosis are caused by mutation in the alpha- spectrin gene (MIM 182860), the beta- spectrin gene (MIM 182870), or the band 3 gene (MIM 109270) [supplied by OMIM].
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 coat. This enables them to circulate without adhering to other cells or vessel ...
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 ...
Red blood cells, or erythrocytes, have a unique lipid composition. The bilayer of red blood cells is composed of cholesterol and phospholipids in equal proportions by weight. [7] Erythrocyte membrane plays a crucial role in blood clotting. In the bilayer of red blood cells is phosphatidylserine. [8]
This became known as a red blood cell "ghost" (spectre), and so the major protein of the ghost was named spectrin. In certain types of brain injury such as diffuse axonal injury, spectrin is irreversibly cleaved by the proteolytic enzyme calpain, destroying the cytoskeleton. [2] Spectrin cleavage causes the membrane to form blebs and ultimately ...
Alfred Gottschalk proved in 1957 that hemagglutinins bind a virus to a host cell by attaching to sialic acids on carbohydrate side chains of cell-membrane glycoproteins and glycolipids. [11] The name "hemagglutinin" comes from the protein's ability to cause red blood cells (erythrocytes) to clump together ("agglutinate") in vitro. [12]
11826 Ensembl ENSG00000240583 ENSMUSG00000004655 UniProt P29972 Q6JSD8 Q6JSD7 Q02013 RefSeq (mRNA) NM_198098 NM_000385 NM_001185060 NM_001185061 NM_001185062 NM_001329872 NM_007472 RefSeq (protein) NP_001316801 NP_932766 NP_031498 Location (UCSC) Chr 7: 30.91 – 30.93 Mb Chr 6: 55.31 – 55.33 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Aquaporin 1 (AQP-1) is a protein that in ...
Fluid mosaic model of a cell membrane. The fluid mosaic model explains various characteristics regarding the structure of functional cell membranes.According to this biological model, there is a lipid bilayer (two molecules thick layer consisting primarily of amphipathic phospholipids) in which protein molecules are embedded.