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CD59 glycoprotein, also known as MAC-inhibitory protein (MAC-IP), membrane inhibitor of reactive lysis (MIRL), or protectin, is a protein that in humans is encoded by the CD59 gene. [5] It is an LU domain and belongs to the LY6/uPAR/alpha-neurotoxin protein family. [6] CD59 attaches to host cells via a glycophosphatidylinositol (GPI) anchor.
Hemolysins or haemolysins are lipids and proteins that cause lysis of red blood cells by disrupting the cell membrane.Although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infection.
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 ...
A red blood cell in a hypotonic solution, causing water to move into the cell A red blood cell in a hypertonic solution, causing water to move out of the cell. Hemolysis or haemolysis (/ h iː ˈ m ɒ l ɪ s ɪ s /), [1] also known by several other names, is the rupturing of red blood cells (erythrocytes) and the release of their contents into surrounding fluid (e.g. blood plasma).
These functions are highly dependent on the membrane composition. The red blood cell membrane is composed of 3 layers: the glycocalyx on the exterior, which is rich in carbohydrates; the lipid bilayer which contains many transmembrane proteins, besides its lipidic main constituents; and the membrane skeleton, a structural network of proteins ...
Immunocytochemistry labels individual proteins within cells, such as TH (green) in the axons of sympathetic autonomic neurons. Immunocytochemistry (ICC) is a common laboratory technique that is used to anatomically visualize the localization of a specific protein or antigen in cells by use of a specific primary antibody that binds to it.
It is also found in some plant proteins responsible for boron transport. [5] In these proteins it covers almost the entire length of the sequence. The Band 3 anion exchange proteins that exchange bicarbonate are the most abundant polypeptide in the red blood cell membrane, comprising 25% of the total membrane protein. The cytoplasmic domain of ...
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]