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生物源
bovine milk
品質等級
形狀
powder
分子量
~14.2 kDa
包裝
vial of 5 mg
技術
electrophoresis: suitable
溶解度
H2O: soluble 10 mg/mL
UniProt登錄號
儲存溫度
2-8°C
基因資訊
cow ... LALBA(281894)
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一般說明
α-乳清蛋白是一种分子量较小的球状乳清蛋白，存在于迄今为止已研究的所有乳汁中。它是在乳腺中产生的大约 14 kDa 的金属蛋白。
應用
牛乳中的 α-乳清蛋白适用于：
- 作为电泳标记，摩尔质量约为 14,200Da
- 通过反向电荷奇偶性模型研究蛋白质在带电表面氧化铁纳米颗粒上的选择性结合
生化／生理作用
α-乳清蛋白由具有 8 个半胱氨酸的单条多肽链组成，这些半胱氨酸形成二硫键。α-乳清蛋白结合包括钙在内的几种金属离子，人们认为该结合在从还原的变性形式的 α-乳清蛋白再生成天然 α-乳清蛋白的过程中发挥作用。α-乳清蛋白还具有独特的锌结合位点，其被认为在乳糖合酶复合物的结合中起作用。 其成熟蛋白由 123 个氨基酸残基（14kD）组成，具有 1.7 埃分辨率的三维结构，包含四个 α-螺旋和三链反平行 β-折叠。
其可通过改变半乳糖基转移酶的底物特异性以增加乳糖形成的速率；半乳糖基转移酶和α-乳白蛋白的复合物称为乳糖合酶。Asp87 或 Asp88 对 Ala 的定点诱变完全消除了强钙结合亲和力，并将乳糖合酶的刺激降低到最大速率的 <3.5%。
其他客户在看
Guanhao Bu et al.
Journal of the science of food and agriculture, 90(12), 2015-2020 (2010-06-29)
The main whey proteins alpha-lactalbumin (alpha-LA) and beta-lactoglobulin (beta-LG) are considered as the major allergens in cow's milk. Microbial fermentation can produce some proteolytic enzymes, which can induce the degradation of milk protein allergens. In this study, the effects of
Haidong Tan et al.
Biotechnology letters, 27(16), 1177-1182 (2005-09-15)
Recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) was produced in E. coli as an inclusion body. rHuIL-1ra was purified to Over 98% purity by anion exchange chromatography after on-column refolding. The optimized processes produced more than 2 g pure refolded rHuIL-1ra
Selective binding of proteins on functional nanoparticles via reverse charge parity model: an in vitro study.
Ghosh G, et, al.
Materials Research Express, 1 (2014)
S Yefimov et al.
Journal of biochemical and biophysical methods, 42(1-2), 65-78 (2000-01-27)
Five SDS-proteins, ranging in molecular weight from 14 to 66 kDa, were detected without covalent fluorescent labeling by the automated gel electrophoresis apparatus with intermittent fluorescence scanning (HPGE apparatus, LabIntelligence) during electrophoresis in barbiturate buffer in the presence of Cascade
Eric Lorent et al.
Vaccine, 26(3), 399-410 (2007-12-14)
The structure of the ectodomain of the hepatitis C envelope glycoprotein E1 (E1s) was characterised by spectroscopic methods. Monomeric E1s was purified from a mammalian and from a Hansenula polymorpha cell lysate, and cysteine-blocked monomers were reconstituted into stable particles.
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