Identification of human plasma proteins as major clients for the extracellular chaperone clusterin

Journal of Biological Chemistry

Volumn 285, Issue 6, 2010, Pages 3532-3539

  Wyatt, Amy R ^a   Wilson, Mark R ^a  

^a UNIVERSITY OF WOLLONGONG   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

BLOT ANALYSIS; CERULOPLASMINS; CLUSTERIN; DISEASE-ASSOCIATED PROTEINS; ENZYME LINKED IMMUNOSORBENT ASSAY; EXTRACELLULAR; EXTRACELLULAR PROTEINS; HIGH MOLECULAR WEIGHT; HUMAN PLASMA PROTEINS; IMMUNOAFFINITY CHROMATOGRAPHY; IN-SITU; IN-VIVO; PLASMA SAMPLES; RECEPTOR-MEDIATED ENDOCYTOSIS; SDS-PAGE; SOLUBLE PROTEINS; WESTERN-BLOT ANALYSIS;

CUSTOMER SATISFACTION; DYES; GLYCOPROTEINS; IDENTIFICATION (CONTROL SYSTEMS); MASS SPECTROMETRY; MOLECULAR WEIGHT; PHYSIOLOGICAL MODELS; PLASMA DEPOSITION; PLASMAS; PROTEIN FOLDING; PURIFICATION; SIZE EXCLUSION CHROMATOGRAPHY; TOTAL QUALITY MANAGEMENT;

QUALITY CONTROL;

ALBUMIN; CERULOPLASMIN; CLUSTERIN; FIBRINOGEN; PLASMA PROTEIN; CHAPERONE; SERUM ALBUMIN;

ARTICLE; BLOOD ANALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; ENDOCYTOSIS; ENZYME LINKED IMMUNOSORBENT ASSAY; GEL PERMEATION CHROMATOGRAPHY; HUMAN; IMMUNOAFFINITY CHROMATOGRAPHY; IMMUNOBLOTTING; MASS SPECTROMETRY; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN PURIFICATION; SHEAR STRESS; WESTERN BLOTTING; AFFINITY CHROMATOGRAPHY; CHEMISTRY; EXTRACELLULAR SPACE; GEL CHROMATOGRAPHY; MECHANICAL STRESS; METABOLISM; METHODOLOGY; PROTEIN BINDING; PROTEOMICS; TEMPERATURE;

BLOOD PROTEINS; BLOTTING, WESTERN; CERULOPLASMIN; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, GEL; CLUSTERIN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; EXTRACELLULAR SPACE; FIBRINOGEN; HUMANS; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEOMICS; SERUM ALBUMIN; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STRESS, MECHANICAL; TEMPERATURE;

EID: 77949292454     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.079566     Document Type: Article

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