Inequivalent contribution of the five tryptophan residues in the C-Lobe of human serum transferrin to the fluorescence increase when iron is released

Biochemistry

Volumn 48, Issue 13, 2009, Pages 2858-2867

  James, Nicholas G ^a   Byrne, Shaina L ^a   Steere, Ashley N ^a   Smith, Valerie C ^b   MacGillivray, Ross T A ^b   Mason, Anne B ^a  

^a UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; CLATHRIN-COATED VESICLES; CONFORMATIONAL CHANGES; ENDOSOME; FLUORESCENT SIGNALS; HUMAN SERUM TRANSFERRIN (HTF); HUMAN SERUM TRANSFERRINS; INTRINSIC FLUORESCENCE SIGNALS; IRON RELEASE; RECEPTOR-MEDIATED ENDOCYTOSIS; TIME-SCALE; TRYPTOPHAN RESIDUES;

AMINO ACIDS; BODY FLUIDS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; IRON COMPOUNDS;

RATE CONSTANTS;

ANION; CHELATING AGENT; CLATHRIN; FERRIC ION; MEMBRANE RECEPTOR; TRANSFERRIN; TRYPTOPHAN;

ANIMAL CELL; ARTICLE; BINDING SITE; CELL SURFACE; CELL VACUOLE; COMPLEX FORMATION; CONFORMATION; CRYSTAL STRUCTURE; ENDOCYTOSIS; ENDOSOME; EVALUATION; FLUORESCENCE; IRON TRANSPORT; MUTANT; NONHUMAN; PH; PRIORITY JOURNAL; RECEPTOR BINDING; SIGNAL TRANSDUCTION; TRANSFERRIN BLOOD LEVEL;

ABSORPTION; CRYSTALLOGRAPHY, X-RAY; FLUORESCENCE; HUMANS; IRON; KINETICS; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, TRANSFERRIN; SERUM; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFERRIN; TRYPTOPHAN;

EID: 65249143886     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8022834     Document Type: Article

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