Bovine serum albumin

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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
Bovine serum albumin 3v03 crystal structure.jpg
Identifiers
Organism Bos taurus (domestic cow)
Symbol ALB
Entrez 280717
RefSeq (mRNA) NM_180992
RefSeq (Prot) NP_851335
UniProt P02769
Other data
Chromosome 6: 91.54 - 91.57 Mb

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 in lab experiments.

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.

Properties[edit]

The full-length BSA precursor protein is 607 amino acids(AAs) in length. An 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 are cleaved to yield the mature BSA protein that contains 583 amino acids.[citation needed]

Peptide Position Length (AAs) MW Da
Full length precursor  1 – 607 607 69,324
Signal peptide  1 –  18 18 2,107
Propeptide 19 –  22 4 478
Mature protein 25 – 607 583 66,463

Physical properties of BSA:

  • Number of amino acid residues: 583
  • Molecular weight: 66,463 Da (= 66.5 kDa)
  • isoelectric point in water at 25 °C: 4.7[1]
  • Extinction coefficient of 43,824 M−1cm−1 at 279 nm[2]
  • Dimensions: 140 × 40 × 40 Å (prolate ellipsoid where a = b < c)[3]
  • pH of 1% Solution: 5.2-7 [4][5]
  • Optical Rotation: [α]259: -61°; [α]264: -63°[5][4]
  • Stokes Radius (rs): 3.48 nm[6]
  • Sedimentation constant, S20,W × 1013: 4.5 (monomer), 6.7 (dimer)[5][4]
  • Diffusion constant, D20,W × 107 cm2/s: 5.9[5][4]
  • Partial specific volume, V20: 0.733[5][4]
  • Intrinsic viscosity, η: 0.0413[5][4]
  • Frictional ratio, f/f0: 1.30[5][4]
  • Refractive index increment (578 nm) × 10-3: 1.90[5][4]
  • Optical absorbance, A279nm1 g/L: 0.667[5][4]
  • Mean residue rotation, [m']233: 8443[5][4]
  • Mean residue ellipticity: 21.1 [θ]209 nm; 20.1 [θ]222 nm[5][4]
  • Estimated a-helix, %: 54[5][4]
  • Estimated b-form, %: 18[5][4]

Applications[edit]

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.[7] 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[edit]

References[edit]

  1. ^ Ge S, Kojio K, Takahara A, Kajiyama T (1998). "Bovine serum albumin adsorption onto immobilized organotrichlorosilane surface: influence of the phase separation on protein adsorption patterns". J Biomater Sci Polym Ed. 9 (2): 131–50. PMID 9493841. 
  2. ^ Peters T (1975). Putman FW, ed. The Plasma Proteins. Academic Press. pp. 133–181. 
  3. ^ Wright AK, Thompson MR (February 1975). "Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence". Biophys. J. 15 (2 Pt 1): 137–41. doi:10.1016/S0006-3495(75)85797-3. PMC 1334600. PMID 1167468. 
  4. ^ a b c d e f g h i j k l m Putnam FW (1975). The Plasma Proteins: Structure, Function and Genetic Control 1 (2nd ed.). New York: Academic Press. p. 141, 147. ASIN B007ESU1JQ. 
  5. ^ a b c d e f g h i j k l m "Albumin from bovine serum". Sigma-Aldrich. Retrieved 5 July 2013. 
  6. ^ Axelsson I (May 1978). "Characterization of proteins and other macromolecules by agarose gel chromatography". Journal of Chromatography A 152 (1): 21–32. doi:10.1016/S0021-9673(00)85330-3. 
  7. ^ "BSA FAQ". Invitrogen. Retrieved 19 January 2012. 

Further reading[edit]

External links[edit]