Site accessibility and the pH dependence of the saturation capacity of a highly cross-linked matrix. Immobilized metal affinity chromatography of bovine serum albumin on chelating Superose

Journal of Chromatography A

Volumn 767, Issue 1-2, 1997, Pages 11-23

  Patwardhan, Anshuman V ^b   Ataai, Mohammad M ^a,b  

^a UNIVERSITY OF PITTSBURGH   (United States)

^b University of Pittsburgh   (United States)

Author keywords

Adsorption isotherms; Albumin; Immobilized metal ion affinity chromatography; pH effects; Proteins; Saturation capacity; Stationary phases, LC

Indexed keywords

BOVINE SERUM ALBUMIN;

ADSORPTION; AFFINITY CHROMATOGRAPHY; ARTICLE; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PURIFICATION; TECHNIQUE; THEORY;

BINDING SITES; CHELATING AGENTS; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, AGAROSE; COPPER; HYDROGEN-ION CONCENTRATION; METALS; SERUM ALBUMIN, BOVINE;

BOVINAE;

EID: 0030965821     PISSN: 00219673     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0021-9673(97)00013-7     Document Type: Article

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