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使用DEAE-亲和凝胶蓝纯化转铁蛋白和乳铁蛋白。

Purification of transferrins and lactoferrin using DEAE affi-gel blue.

作者信息

Chung M C, Chan S L, Shimizu S

机构信息

Department of Biochemistry, National University of Singapore.

出版信息

Int J Biochem. 1991;23(5-6):609-16.

PMID:2065820
Abstract
  1. A simple method for purifying transferrins and lactoferrin is described. 2. The method consists of a preliminary step of dye-ligand chromatography using DEAE Affi-Gel Blue as the gel matrix at pH 7.5. In this chromatographic step, the transferrins and lactoferrin were readily separated from the bulk of the other proteins by start buffer elution. 3. Differences in the chromatographic behaviour of the various serum transferrins (monkey, human, rabbit, pig, chicken and duck) and ovotransferrin upon DEAE Affi-Gel Blue chromatography can be attributed to differences in the anionic charge of the transferrins in 0.02 M potassium phosphate buffer, pH 7.5, thus resulting in the differential retardation of these protein molecules by the gel matrix. 4. The result of DEAE Affi-Gel Blue chromatography of human lactoferrin is different from that for the transferrins. This may possibly reflect the differences in the strength of interaction between lactoferrin and transferrin with this gel matrix.
摘要
  1. 描述了一种纯化转铁蛋白和乳铁蛋白的简单方法。2. 该方法包括一个初步步骤,即在pH 7.5条件下使用DEAE亲和凝胶蓝作为凝胶基质进行染料配体色谱法。在这一色谱步骤中,通过起始缓冲液洗脱,转铁蛋白和乳铁蛋白很容易与其他大部分蛋白质分离。3. 各种血清转铁蛋白(猴、人、兔、猪、鸡和鸭)和卵转铁蛋白在DEAE亲和凝胶蓝色谱上的色谱行为差异,可归因于在pH 7.5的0.02 M磷酸钾缓冲液中转铁蛋白阴离子电荷的差异,从而导致这些蛋白质分子被凝胶基质不同程度地阻滞。4. 人乳铁蛋白的DEAE亲和凝胶蓝色谱结果与转铁蛋白不同。这可能反映了乳铁蛋白和转铁蛋白与这种凝胶基质相互作用强度的差异。

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