A new process of IgG purification by negative chromatography: Adsorption aspects of human serum proteins onto ω-aminodecyl-agarose

Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences

Volumn 878, Issue 23, 2010, Pages 2087-2093

  Bresolin, Igor Tadeu Lazzarotto ^a   de Souza, Maria Cristiane Martins ^a   Bueno, Sonia Maria Alves ^a  

^a UNIVERSITY OF CAMPINAS   (Brazil)

Author keywords

Aminodecyl agarose; Adsorption; Human IgG; Mixed mode interactions; Purification

Indexed keywords

AGAROSE; BUFFER SYSTEM; COOPERATIVE EFFECTS; COOPERATIVITY; HIGH PURITY; HUMAN IGG; HUMAN SERUM; HUMAN SERUM ALBUMINS; HUMAN SERUM PROTEINS; HYDROPHOBIC INTERACTIONS; IMMUNOGLOBULIN G; MIXED MODE; MIXED-MODE INTERACTIONS; NEW PROCESS; PLASMA PROTEIN; POTENTIAL TECHNIQUES; SERUM PROTEINS; TOTAL PROTEIN CONCENTRATION;

ADSORPTION; BODY FLUIDS; HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBICITY; PURIFICATION;

PROTEINS;

ADSORBENT; BUFFER; HUMAN SERUM ALBUMIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; OMEGA AMINODECYL AGAROSE; TRANSFERRIN; UNCLASSIFIED DRUG; PLASMA PROTEIN; PROTEIN BINDING; SEPHAROSE; SERUM ALBUMIN; SOLUTION AND SOLUBILITY;

ARTICLE; CHEMICAL INTERACTION; CHROMATOGRAPHY; CONTROLLED STUDY; HUMAN; ISOTHERM; NORMAL HUMAN; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PURIFICATION; ADSORPTION; ANALOGS AND DERIVATIVES; CHEMICAL MODEL; CHEMISTRY; ISOELECTRIC FOCUSING; ISOELECTRIC POINT; ISOLATION AND PURIFICATION; KINETICS; OXIDATION REDUCTION REACTION; PHOTOMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROCEDURES; SERUM; SOLUTION AND SOLUBILITY; TEMPERATURE;

ADSORPTION; BLOOD PROTEINS; BUFFERS; CHROMATOGRAPHY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN G; ISOELECTRIC FOCUSING; ISOELECTRIC POINT; KINETICS; MODELS, CHEMICAL; NEPHELOMETRY AND TURBIDIMETRY; OXIDATION-REDUCTION; PROTEIN BINDING; SEPHAROSE; SERUM; SERUM ALBUMIN; SOLUTIONS; TEMPERATURE;

EID: 77955058243     PISSN: 15700232     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jchromb.2010.06.009     Document Type: Article

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