WordNet

a book of blank pages with pockets or envelopes; for organizing photographs or stamp collections etc
one or more recordings issued together; originally released on 12-inch phonograph records (usually with attractive record covers) and later on cassette audiotape and compact disc (同)record album
dull and slow-moving and stolid; like an ox; "showed a bovine apathy"
any of various members of the genus Bos
of or relating to or belonging to the genus Bos (cattle) (同)bovid
a simple water-soluble protein found in many animal tissues and liquids (同)albumen
an amber, watery fluid, rich in proteins, that separates out when blood coagulates (同)blood_serum

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(写真・切手・切り抜きなどを貼る)『アルバム』 / (いくつかの曲・劇などを収録した)組レコード,アルバム / 画帳
牛の;牛のような / のっそりした,鈍重な / ウシ科の動物
アルブミン(蛋白質の一種)
リンパ液 / 血清
serial / series / sermon

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/03 11:04:35」(JST)

wiki en

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.

Lyophilized Bovine Serum Albumin

Properties

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°^[4]^[5]
Stokes Radius (r_s): 3.48 nm^[6]
Sedimentation constant, S_20,W × 10¹³: 4.5 (monomer), 6.7 (dimer)^[4]^[5]
Diffusion constant, D_20,W × 10^-7 cm²/s: 5.9^[4]^[5]
Partial specific volume, V₂₀: 0.733^[4]^[5]
Intrinsic viscosity, η: 0.0413^[4]^[5]
Frictional ratio, f/f0: 1.30^[4]^[5]
Refractive index increment (578 nm) × 10⁻³: 1.90^[4]^[5]
Optical absorbance, A^279 nm_1 g/L: 0.667^[4]^[5]
Mean residue rotation, [m']₂₃₃: 8443^[4]^[5]
Mean residue ellipticity: 21.1 [θ]_209 nm; 20.1 [θ]_222 nm^[4]^[5]
Estimated a-helix, %: 54^[4]^[5]
Estimated b-form, %: 18^[4]^[5]

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. 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.

References

^ 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". Journal of Biomaterials Science. Polymer Edition 9 (2): 131–50. doi:10.1163/156856298x00479. PMID 9493841.
^ Peters T (1975). Putman FW, ed. The Plasma Proteins. Academic Press. pp. 133–181.
^ Wright AK, Thompson MR (Feb 1975). "Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence". Biophysical Journal 15 (2 Pt 1): 137–41. doi:10.1016/S0006-3495(75)85797-3. PMC 1334600. PMID 1167468.
^ ^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. pp. 141, 147. ASIN B007ESU1JQ.
^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m "Albumin from bovine serum" (PDF). Sigma-Aldrich. Retrieved 5 July 2013.
^ 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.
^ "BSA FAQ". Invitrogen. Retrieved 19 January 2012.

External links

Serum Albumin, Bovine at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

Dose- and time-dependent effect of copper ions on the viability of bull spermatozoa in different media.

Knazicka Z, Tvrda E, Bardos L, Lukac N.Sourcea Department of Animal Physiology , Slovak University of Agriculture , Nitra , Slovak Republic.
Journal of environmental science and health. Part A, Toxic/hazardous substances & environmental engineering.J Environ Sci Health A Tox Hazard Subst Environ Eng.2012 Jul 15;47(9):1294-300.
The purpose of this in vitro study was to determine the effect of copper (Cu) on the motility and viability of spermatozoa in the presence of different culture media. Specifically, we examined the dose- and time-dependent effect of copper ions (Cu(2+)) on the motility and viability of spermatozoa du
PMID 22540654

A linear-dendritic cationic vector for efficient DNA grasp and delivery.

Yang B, Sun YX, Yi WJ, Yang J, Liu CW, Cheng H, Feng J, Zhang XZ, Zhuo RX.SourceKey Laboratory of Biomedical Polymers (Ministry of Education), Department of Chemistry, Wuhan University, Wuhan 430072, People's Republic of China.
Acta biomaterialia.Acta Biomater.2012 Jul;8(6):2121-32. Epub 2012 Feb 25.
This paper presents an attempt to design an efficient and biocompatible cationic gene vector via structural optimization that favors the efficient utilization of amine groups for DNA condensation. To this end, a linear-dendritic block copolymer of methoxyl-poly(ethylene glycol)-dendritic polyglycero
PMID 22370448

Japanese Journal

Small heat shock protein AgsA : An effective stabilizer of enzyme activities

Tomoyasu Toshifumi,Tabata Atsushi,Ishikawa Yoko
Journal of bioscience and bioengineering 115(1), 15-19, 2013-01
NAID 40019555502

Sol-gel preparation of apatite-coated silica macrospheres from water glass and their adsorption of bovine serum albumin and lysozyme

LI Jie,SHIROSAKI Yuki,HAYAKAWA Satoshi
Journal of the Ceramic Society of Japan 120(1405), 355-361, 2012-09
NAID 40019396442

Related Pictures

★リンクテーブル★

リンク元	「BSA」「ウシ血清アルブミン」
関連記事	「bovine」「bovine serum」

「BSA」

albumin
Identifiers
Organism	Bos taurus (domestic cow)
Symbol	ALB
Entrez	280717
HomoloGene	105925
RefSeq (mRNA)	NM_180992
RefSeq (Prot)	NP_851335
UniProt	P02769
Other data
Chromosome	6: 91.54 - 91.57 Mb

　　[★]

「ウシ血清アルブミン」

　　[★]

英: bovine serum albumin、BSA

「bovine」

　　[★]

ウシの

関: Bos taurus、cattle、ox、oxen

「bovine serum」

　　[★]

ウシ血清

関: calf serum

[pmid9493841-1] 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". Journal of Biomaterials Science. Polymer Edition 9 (2): 131–50. doi:10.1163/156856298x00479. PMID 9493841.

[Peters_1975-2] Peters T (1975). Putman FW, ed. The Plasma Proteins. Academic Press. pp. 133–181.

[pmid1167468-3] Wright AK, Thompson MR (Feb 1975). "Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence". Biophysical Journal 15 (2 Pt 1): 137–41. doi:10.1016/S0006-3495(75)85797-3. PMC 1334600. PMID 1167468.

[Putman_1975-4] ^ ^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. pp. 141, 147. ASIN B007ESU1JQ.

[Sigma-Aldrich_ref01-5] ^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k ^l ^m "Albumin from bovine serum" (PDF). Sigma-Aldrich. Retrieved 5 July 2013.

[Axelsson_1978-6] 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.

匿名

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案内

案内

bovine serum albumin