From Wikipedia, the free encyclopedia
gamma-Amanitin or γ-amanitin is a
of eight . It is an , a group of
isolated from and found in several members of the
genus of , one being the Death cap () as well as the , a complex of similar species, principally
[[Category:Sulfoxides]
article is a . You can help Wikipedia by .
: Hidden categories:From Wikipedia, the free encyclopedia
This article may require
to meet Wikipedia's . The specific problem is: Improved diagram in structure section needed. Please help
if you can. (November 2016) ()
This article needs additional citations for . Please help
by . Unsourced material may be challenged and removed. (March 2009) ()
The albumins (formed from : albumen "(egg) dried egg white") are a
of , the most common of which are the . All the proteins of the albumin family are water-, moderately soluble in concentrated salt solutions, and experience heat . Albumins are commonly found in
and differ from other
in that they are not . Substances containing albumins, such as , are called albuminoids.
A number of blood
are evolutionarily related, including serum albumin, ,
Albumin binds to the cell surface receptor .
Serum albumin is the main protein of human blood plasma. It binds water, cations (such as Ca2+, Na+ and K+), , hormones, , thyroxine (T4) and pharmaceuticals (including barbiturates): its main function is to regulate the
(alpha-fetoglobulin) is a fetal plasma protein that binds various cations, fatty acids and bilirubin.
binds to vitamin D and its metabolites, as well as to fatty acids. The
of albumin is 4.9.
The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 ?ngstr?ms (250 pm). Albumin is a 65–70
Albumin comprises three homologous domains that assemble to form a heart-shaped protein. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds, as shown schematically below:
xxCxxxxxxxxxxxxxxxxCCxxCxxxxCxxxxxCCxxxCxxxxxxxxxCxxxxxxxxxxxxxxCCxxxxCxxxx
+-----------------+
+---------------+
C = cysteine, x = any amino acid
Serum albumin is the most abundant
protein and is produced in the
and forms a large proportion of all plasma protein. The human version is , and it normally constitutes about 50% of
plasma protein.
Serum albumins are important in regulating blood volume by maintaining the
(also known as ) of the blood compartment. They also serve as carriers for molecules of low water solubility this way isolating their hydrophobic nature, including lipid-soluble hormones,
salts, , free
(), , ions (), and some drugs like warfarin, phenobutazone, clofibrate & phenytoin. For this reason, it is sometimes referred as a molecular "taxi". Competition between drugs for albumin binding sites may cause drug interaction by increasing the free fraction of one of the drugs, thereby affecting potency.
Specific types include:
(cattle serum albumin) or BSA, often used in medical and molecular biology labs.
Normal range of human serum albumin in adults (& 3 y.o.) is 3.5 to 5 g/dL. For children less than three years of age, the normal range is broader, 2.9–5.5 g/dL.
Low albumin () may be caused by , , burns, , , , late pregnancy, artefact, genetic variations and malignancy.
High albumin () is almost always caused by dehydration. In some cases of
() deficiency, the albumin level can be elevated to high-normal values (e.g., 4.9 g/dL). This is because retinol causes cells to swell with water (this is also the reason too much Vitamin A is toxic). This swelling also likely occurs during treatment with 13-cis retinoic acid (), a pharmaceutical for treating severe acne, amongst other conditions. In lab experiments it has been shown that all-trans retinoic acid down regulates human albumin production
Other albumin types include the
in egg white, and different storage albumins in the
of some , including .
Note that the protein "albumin" is spelled with an "i", while "albumen" with an "e", is the white of an egg, which contains (among other things) several dozen types of albumin (with an "i"), mostly .
For patients with low blood volume, there is no evidence that albumin reduces mortality when compared with cheaper alternatives such as , or that albumin reduces mortality in patients with burns and low albumin levels. Therefore, the
recommends that it not be used, except in .[]
(ADV), albumin is sometimes used as a . ADV has been proposed as a cancer treatment by means of .
Worldwide, certain traditional Chinese medicines contain wild bear bile, banned under
legislation. Dip sticks, similar to common pregnancy tests, have been developed to detect the presence of bear albumin in traditional medicine products, indicating that bear bile had been used in their creation.
(human serum albumin purification method)
This article incorporates text from the
Sugio, S.; Kashima, A.; Mochizuki, S.; Noda, M.; Kobayashi, K. (1 June 1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Engineering Design and Selection. 12 (6): 439–446. :.  .
He, Xiao M Carter, Daniel C. (16 July 1992). "Atomic structure and chemistry of human serum albumin". Nature. 358 (6383): 209–215. :.  .
Pliny The Elder. Historia Naturalis 28, 6, 18.
Haefliger, Denise N Moskaitis, John E.; Schoenberg, Daniel R.; Wahli, Walter (October 1989). "Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family". Journal of Molecular Evolution. 29 (4): 344–354. :.  .
Schoentgen, Franc? Metz-Boutique, Marie-Hélè Jollès, J Constans, J Jollès, Pierre (June 1986). "Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and α-fetoprotein". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 871 (2): 189–198. :.  .
Lichenstein, HS; Lyons, DE; Wurfel, MM; Johnson, DA; McGinley, MD; Leidli, JC; Trollinger, DB; Mayer, JP; Wright, SD; Zukowski, MM (8 July 1994). "Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family". The Journal of Biological Chemistry. 269 (27): 18149–54.  .
Farrugia, Albert (January 2010). "Albumin Usage in Clinical Medicine: Tradition or Therapeutic?". Transfusion Medicine Reviews. 24 (1): 53–63. :.  .
Sugio, S.; Kashima, A.; Mochizuki, S.; Noda, M.; Kobayashi, K. (1 June 1999). . Protein Engineering Design and Selection. 12 (6): 439–446. :.  .
. Archived from the original on .
Pasantes-Morales, H; Wright, CE; Gaull, GE (December 1984). "Protective effect of taurine, zinc and tocopherol on retinol-induced damage in human lymphoblastoid cells". The Journal of Nutrition. 114 (12): 2256–61.  .
Masaki, T; Matsuura, T; Ohkawa, K; Miyamura, T; Okazaki, I; Watanabe, T; Suzuki, T (15 July 2006). . The Biochemical Journal. 397 (2): 345–53. :.   .  .
Roberts I, Blackhall K, Alderson P, Bunn F, Schierhout G (9 November 2011). "Human albumin solution for resuscitation and volume expansion in critically ill patients". The Cochrane database of systematic reviews (11): CD001208. :.  .
Lo, A Kripfgans, O Carson, P Rothman, E Fowlkes, J. (May 2007). "Acoustic droplet vaporization threshold: effects of pulse duration and contrast agent". IEEE Transactions on Ultrasonics, Ferroelectrics and Frequency Control. 54 (5): 933–946. :.
Peppin, McEwing, Webster, Rogers, Nicholls, Ogden 2008 'Development of a field test for the detection of illegal bear products' Endangered Forensics Research (9)
has the text of the
at the US National Library of Medicine
: Hidden categories: