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Open AccessJournal ArticleDOI

Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads.

Pedro Cuatrecasas
- 25 Jun 1970 - 
- Vol. 245, Iss: 12, pp 3059-3065
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TLDR
It is demonstrated that successful application of affinity chromatography in many cases will critically depend on placing the ligand at a considerable distance from the matrix backbone.
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This article is published in Journal of Biological Chemistry.The article was published on 1970-06-25 and is currently open access. It has received 2603 citations till now. The article focuses on the topics: Agarose & Affinity chromatography.

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Book

Isolation and characterization

TL;DR: Animal Models and Therapy, Directed Differentiation and Characterization of Genetically Modified Embryonic Stem Cells for Therapy, and Use of Differentiating Embryonics Stem cells in the Parkinsonian Mouse Model are reviewed.
Journal ArticleDOI

A simplified method for cyanogen bromide activation of agarose for affinity chromatography

TL;DR: Agarose can be activated by adding cyanogen bromide, dissolved in acetonitrile, to beads suspended in a solution of sodium carbonate, and the necessity for manual titration and the use of a pH meter are eliminated.
Book ChapterDOI

[31] Affinity chromatography

TL;DR: Inherent advantages of this method of purification are the rapidity and ease of a potentially single-step procedure, the rapid separation of the protein to be purified from inhibitors and destructive contaminants, such as proteases, and protection from denaturation during purification by active site ligand-stabilization of protein tertiary structure.
Book ChapterDOI

The interactions of lectins with animal cell surfaces.

TL;DR: This chapter discusses the interactions of lectins with animal cell surfaces, which have proven to be quite useful for clinical blood typing and structural studies of blood group substances, in analysis of the surface structure of normal and tumor cells, and so on.
Patent

Process for the demonstration and determination of reaction components having specific binding affinity for each other

TL;DR: In this article, a process for the determination of a component of the reaction between a specific binding protein and the substance being specifically bound by such a protein comprising reacting the component to be determined with its binding partner in an insolubilized form, separating the solid phase of a reaction mixture from the liquid phase, reacting with a determined amount of a coupling product of the substance, and finally determining the enzyme activity of the liquid or solid phase obtained.
References
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Journal ArticleDOI

Tissue sulfhydryl groups

TL;DR: A water-soluble (at pH 8) aromatic disulfide [5,5′-dithiobis(2-nitrobenzoic acid] has been synthesized and shown to be useful for determination of sulfhydryl groups.
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Chemical Coupling of Peptides and Proteins to Polysaccharides by Means of Cyanogen Halides

TL;DR: Biologically active proteins and polypeptides can be coupled by various means to cellulose, starch and cross-linked polysaccharide gels such as ‘Sephadex’.
Journal ArticleDOI

Selective enzyme purification by affinity chromatography

TL;DR: The general principles and potential applications of "affinity chromatography," a protein purification technique that is indispensable to modern biological research, are explained.
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Gel filtration: a method for desalting and group separation.

TL;DR: The method is based on a column procedure similar to chromatography in which the stationary phase is comprised of a new type of gel which consists of hydrophilic chains which are cross-linked.
Journal ArticleDOI

Chemical Coupling of Proteins to Agarose

TL;DR: This method of activation and coupling is gentle and therefore particularly useful for the production of immunosorbents and insoluble enzymes.
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