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在不带电荷的琼脂糖衍生物上进行疏水相互作用色谱法。一种模型蛋白的结合,与离子强度、取代基的疏水性以及取代度(通过核磁共振确定)有关。

Hydrophobic interaction chromatography on non-charged Sepharose derivatives. Binding of a model protein, related to ionic strength, hydrophobicity of the substituent, and degree of substitution (determined by NMR).

作者信息

Rosengren J, Pählman S, Glad M, Hjertén S

出版信息

Biochim Biophys Acta. 1975 Nov 18;412(1):51-61.

PMID:1191676
Abstract

A series of agarose gels, substituted with hydrophobic groups, has been synthesized and used for binding studies with the coloured model protein, phycoerythrin. The degrees of substitution for the derivatives can easily be estimated with proton magnetic resonance (NMR). It has been found that the capacity of the derivatives for phycoerythrin increases with increasing hydrophobicity of the substituent, degree of substitution and increasing ionic strength. For column experiments the degree of substitution should lie in the range 40-100 mmol substituent/mol galactose. When it is excessively high, the flow characteristics of the columns are unsatisfactory and difficulties to achieve complete desorption may arise.

摘要

一系列带有疏水基团的琼脂糖凝胶已被合成,并用于与有色模型蛋白藻红蛋白的结合研究。衍生物的取代度可以很容易地用质子磁共振(NMR)来估计。已经发现,衍生物对藻红蛋白的结合能力随着取代基疏水性的增加、取代度的增加和离子强度的增加而增加。对于柱实验,取代度应在40 - 100 mmol取代基/摩尔半乳糖的范围内。当取代度过高时,柱的流动特性不理想,可能会出现难以实现完全解吸的情况。

相似文献

1
Hydrophobic interaction chromatography on non-charged Sepharose derivatives. Binding of a model protein, related to ionic strength, hydrophobicity of the substituent, and degree of substitution (determined by NMR).在不带电荷的琼脂糖衍生物上进行疏水相互作用色谱法。一种模型蛋白的结合,与离子强度、取代基的疏水性以及取代度(通过核磁共振确定)有关。
Biochim Biophys Acta. 1975 Nov 18;412(1):51-61.
2
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Hydrophobic chromatography of beta-galactosidase.β-半乳糖苷酶的疏水色谱法。
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Chromatographic purification of a mammalian histidine decarboxylase on charged and non-charged alkyl derivatives of agarose.
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Hydrophobic interaction chromatography on uncharged Sepharose derivatives. Effects of neutral salts on the adsorption of proteins.在不带电荷的琼脂糖衍生物上进行疏水相互作用色谱法。中性盐对蛋白质吸附的影响。
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Immobilization of enzymes based on hydrophobic interaction. III. Adsorbent substituent density and its impact on the immobilization of beta-amylase.
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