Ovalbumin

from Wikipedia, the free encyclopedia
Ovalbumin ( Gallus gallus )
Ovalbumin (Gallus gallus)
Ribbon model from two sides according to PDB  1OVA

Existing structural data : 1jti , 1ova , 1p1z , 1p4l , 1uhg , 1vac

Mass / length primary structure 385 amino acids ; 42.8  kDa
Identifier
External IDs
Occurrence
Homology family Serpine
Parent taxon Creature

Ovalbumin (abbreviation: OVA ) is the most abundant protein in the albumen of bird eggs (55–65 percent). The function of ovalbumin is not clearly understood, but it is suspected that it is a storage protein. Ovalbumin belongs to the serpins . In contrast to other serpins, ovalbumin is not able to inhibit serine proteases .

Albert Neuberger proved in 1938 that it was a glycoprotein and thus started glycoprotein research.

biosynthesis

The gene for ovalbumin can  be found on chromosome 2 in the domestic chicken ( Gallus gallus domesticus ) and comprises 8 exons and 5900 base pairs (5.9 kbp). The transcribed mRNA contains 1392 bases and after translation and further post-translational modification , the 385 amino acid ovalbumin with a molecular mass of 42.8  kDa is formed . The protein sequence of chicken ovalbumin was fully elucidated in 1981.

use

Ovalbumin has a high status for protein research as it was historically used for the development of techniques for molecular weight measurement and structure elucidation due to its great availability . It still serves as a comparison standard in these areas. Due to its structure similar to the serpins , it is used to research this family of proteins. It is also used in immunology to produce an allergic reaction.

history

Chicken ovalbumin was the second protein (after hemoglobin in 1870) to be presented in pure and crystal form. Franz Hofmeister succeeded in 1889 by carefully precipitating with ammonium sulfate solution to produce pure ovalbumin and to grow crystals from it. The protein was only given its name in 1900 by Osborne and Campbell.

properties

Ovalbumin can cause allergies in people .

Ovalbumin is water repellent . Chicken ovalbumin coagulates at 84.5 ° C

literature

  • F. Hofmeister: On the representation of crystallized egg albumin and the crystallizability of colloid substances. Journal of Physiological Chemistry 14 / - / 1890 . Pp. 165–172 facsimile at MPIWG
  • F. Hofmeister: About the composition of the crystalline egg albumin. Journal of Physiological Chemistry 16 / - / 1892 . Pp. 187–191 facsimile at MPIWG
  • TB Osborne and GF Campbell, J. Am. Chem. Soc. 22 / - / 1900 . P. 422ff

Individual evidence

  1. ↑ Gettins PGW (2002) serpin structure, mechanism, and function. Chemical Reviews 102 (12): 4751-4804.
  2. ^ A. Neuberger: Carbohydrates in protein. In: Biochemical Journal. 32, 1938, pp. 1435-1451, doi : 10.1042 / bj0321435 .
  3. ↑ ENSEMBL entry
  4. ↑ AD Nisbet, RH Saundry et al. a .: The complete amino-acid sequence of hen ovalbumin. In: European Journal of Biochemistry / FEBS. Volume 115, Number 2, April 1981, pp. 335-345, doi : 10.1111 / j.1432-1033.1981.tb05243.x (free full text). PMID 7016535 .
  5. ↑ Information material at Fordras ( Memento of the original from October 2, 2008 in the Internet Archive ) Info: The archive link was automatically inserted and not yet checked. Please check the original and archive link according to the instructions and then remove this notice. @1@ 2Template: Webachiv / IABot / www.fordras.com
  6. ^ Rudolf Hausmann : To Grasp the Essence of Life. A History of Molecular Biology. Springer 2003. ISBN 1-402-01092-3 , p. 10.
  7. ↑ Haskard Carolyn A., Eunice CY Li-Chan: Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS - ) fluorescent probes. Agricultural and Food Chemistry, Vol. 46, No. 7, 1998, pp. 2671-2677, doi : 10.1021 / jf970876y .
  8. ↑ Easter: the festival of the egg .