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Contrary to popular belief, haemoglobin is not a blood protein, as it is carried within red blood cells, rather than in the blood serum. Serum albumin accounts for 55% of blood proteins, [1] is a major contributor to maintaining the oncotic pressure of plasma and assists, as a carrier, in the transport of lipids and steroid hormones.
IGF binding protein, carries insulin-like growth factor 1; Major urinary proteins, carries pheromones in rodents; Retinol binding protein, carries retinol; Sex hormone-binding globulin, carries sex hormones, specifically testosterone and estradiol; Thyroxine-binding globulin, carries the thyroid hormones thyroxine (T4) and 3,5,3 ...
Every carrier protein, especially within the same cell membrane, is specific to one type or family of molecules. GLUT1 is a named carrier protein found in almost all animal cell membranes that transports glucose across the bilayer. This protein is a uniporter, meaning it transports glucose along its concentration in a singular direction. It is ...
Serum albumin, often referred to simply as blood albumin, is an albumin (a type of globular protein) found in vertebrate blood. Human serum albumin is encoded by the ALB gene . [ 2 ] [ 3 ] [ 4 ] Other mammalian forms, such as bovine serum albumin , are chemically similar.
Hemoglobin also transports other gases. It carries off some of the body's respiratory carbon dioxide (about 20–25% of the total) [9] as carbaminohemoglobin, in which CO 2 binds to the heme protein. The molecule also carries the important regulatory molecule nitric oxide bound to a thiol group in the globin protein, releasing it at the same ...
Blood plasma is a light amber-colored liquid component of blood in which blood cells are absent, but which contains proteins and other constituents of whole blood in suspension. It makes up about 55% of the body's total blood volume. [ 1 ]
Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. It was first described in 1948. [ 8 ] Another protein, hephaestin , is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism.
Upon binding and recognition of a specific substrate molecule on one side of the uniporter membrane, a conformational change is triggered in the transporter protein. [27] This causes the transporter protein to change its three-dimensional shape, which ensures the substrate molecule is captured within the transporter proteins structure.