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The nickname "Fraction V" refers to albumin being the fifth fraction of the original [[Cohn process|Edwin Cohn purification methodology]] that made use of differential solubility characteristics of [[plasma protein]]s. By manipulating solvent concentrations, pH, [[salt]] levels, and [[temperature]], Cohn was able to pull out successive "fractions" of [[blood plasma]]. The process was first commercialized with human albumin for medical use and later adopted for production of BSA.
The nickname "Fraction V" refers to albumin being the fifth fraction of the original [[Cohn process|Edwin Cohn purification methodology]] that made use of differential solubility characteristics of [[plasma protein]]s. By manipulating solvent concentrations, pH, [[salt]] levels, and [[temperature]], Cohn was able to pull out successive "fractions" of [[blood plasma]]. The process was first commercialized with human albumin for medical use and later adopted for production of BSA.

== Properties ==

The full-length BSA precursor protein is 607 amino acids in length. An [[N-terminus|N-terminal]] 18-residue [[signal peptide]] is cut off from the precursor protein upon secretion, hence the initial protein product contains 589 amino acid residues. An additional 4 amino acids is cleaved to yield the mature BSA protein that contains 583 amino acids.

{| class="wikitable"
|-
! Peptide !! Position !! Length !! MW [[Atomic mass unit|Da]]
|-
| Full length precursor ||  1 – 607 || align="right" | 607 || align="right" | 69,324
|-
| [[Signal peptide]] ||  1 –  18 || align="right" | 18 || align="right" | 2,107
|-
| Propeptide || 19 –  22 || align="right" | 4 || align="right" | 478
|-
| Mature protein || 25 – 607 || align="right" | 583 || align="right" | 66,463
|}

Physical properties of BSA:
* Number of amino acid residues: 583
* Molecular weight: 66,463 [[Atomic mass unit|Da]] (= 66.5 kDa)
* [[isoelectric point]] in water at 25 °C: 4.7<ref name="pmid9493841">{{cite journal | author = Ge S, Kojio K, Takahara A, Kajiyama T | title = Bovine serum albumin adsorption onto immobilized organotrichlorosilane surface: influence of the phase separation on protein adsorption patterns| journal = J Biomater Sci Polym Ed. | volume = 9 | issue = 2 | pages = 131–50 | year = 1998 | pmid = 9493841| }}</ref>
* Extinction coefficient of 43,824 M<sup>−1</sup>cm<sup>−1</sup> at 279&nbsp;nm<ref name="Peters_1975">{{cite book | editor = Putman FW | author = Peters T | title = The Plasma Proteins | year = 1975 | publisher = Academic Press | pages = 133–181}}</ref>
* Dimensions: 140 X 40 X 40 Å<sup>3</sup> (prolate ellipsoid where a = b < c)<ref name="pmid1167468">{{cite journal | author = Wright AK, Thompson MR | title = Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence | journal = Biophys. J. | volume = 15 | issue = 2 Pt 1 | pages = 137–41 | year = 1975 | month = February | pmid = 1167468 | pmc = 1334600 | doi = 10.1016/S0006-3495(75)85797-3| url = | issn = }}</ref>

* pH of 1% Solution: 5.2-7 <ref name="Putman_1975">{{cite book | author = Putnam FW | title = The Plasma Proteins: Structure, Function and Genetic Control | edition = 2nd | series = | volume = 1 | | year = 1975 | publisher = Academic Press | location = New York | page= 141, 147 | chapter = | chapterurl = | asin = B007ESU1JQ }}</ref><ref name="Sigma-Aldrich ref01">{{cite web|title=Albumin from bovine serum|url=http://www.sigmaaldrich.com/etc/medialib/docs/Sigma/Product_Information_Sheet/b4287pis.Par.0001.File.tmp/b4287pis.pdf|publisher=Sigma-Aldrich|accessdate=5 July 2013}}</ref>
* Optical Rotation: [α]<sub>259</sub>: -61°; [α]<sub>264</sub>: -63°<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Stokes Radius (r<sub>s</sub>): 3.48 nm<ref name=Axelsson_1978>{{cite journal | author = Axelsson I | title = Characterization of proteins and other macromolecules by agarose gel chromatography | journal = Journal of Chromatography A | year = 1978 | month = May | volume = 152 | issue = 1 | pages = 21–32 | doi = 10.1016/S0021-9673(00)85330-3 }}</ref>
* Sedimentation constant, S<sub>20,W</sub> X 10<sup>13</sup>: 4.5 (monomer), 6.7 (dimer)<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Diffusion constant, D<sub>20,W</sub> X 10<sup>7</sup> cm<sup>2</sup>/s: 5.9<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Partial specific volume, V<sub>20</sub>: 0.733<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Intrinsic viscosity, η: 0.0413<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Frictional ratio, f/f0: 1.30<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Refractive index increment (578 nm) X 10<sup>-3</sup>: 1.90<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Optical absorbance, A<sup>279nm</sup><sub>1 gm/L</sub>: 0.667<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Mean residue rotation, [m']<sub>233</sub>: 8443<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Mean residue ellipticity: 21.1 [θ]<sub>209 nm</sub>; 20.1 [θ]<sub>222 nm</sub><ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Estimated a-helix, %: 54<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />
* Estimated b-form, %: 18<ref name="Sigma-Aldrich ref01" /><ref name="Putman_1975" />


== Applications ==
== Applications ==

Revision as of 17:49, 25 July 2013

This article is about albumin specific to cows. For the human variant, see human serum albumin. For the family of mammalian albumins, see serum albumin.
albumin
Identifiers
OrganismBos taurus (domestic cow)
SymbolALB
Entrez280717
RefSeq (mRNA)NM_180992
RefSeq (Prot)NP_851335
UniProtP02769
Other data
Chromosome6: 91.54 - 91.57 Mb
Search for
StructuresSwiss-model
DomainsInterPro

Bovine serum albumin (also known as BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard.

The nickname "Fraction V" refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins. By manipulating solvent concentrations, pH, salt levels, and temperature, Cohn was able to pull out successive "fractions" of blood plasma. The process was first commercialized with human albumin for medical use and later adopted for production of BSA.

Applications

BSA has numerous biochemical applications including ELISAs (Enzyme-Linked Immunosorbent Assay), immunoblots, and immunohistochemistry. It is also used as a nutrient in cell and microbial culture.[citation needed] In restriction digests, BSA is used to stabilize some enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes, pipet tips, and other vessels.[1] This protein does not affect other enzymes that do not need it for stabilization. BSA is also commonly used to determine the quantity of other proteins, by comparing an unknown quantity of protein to known amounts of BSA (see Bradford protein assay). BSA is used because of its stability to increase signal in assays, its lack of effect in many biochemical reactions, and its low cost, since large quantities of it can be readily purified from bovine blood, a byproduct of the cattle industry.

See also

References

  1. ^ "BSA FAQ". Invitrogen. Retrieved 19 January 2012.

Further reading

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