The protease activity of transthyretin reverses the effect of pH on the amyloid-β protein/heparan sulfate proteoglycan interaction: A biochromatographic study

Journal of Pharmaceutical and Biomedical Analysis

Volumn 97, Issue , 2014, Pages 88-96

  Geneste, Ambre ^a   Guillaume, Yves Claude ^a,b   Magy Bertrand, Nadine ^a,b   Lethier, Lydie ^a   Gharbi, T ^a   André, Claire ^a  

^a UNIVERSITÉ DE FRANCHE COMTÉ   (France)

^b UNIVERSITY HOSPITAL OF BESANÇON   (France)

Author keywords

Heparan sulfate proteoglycan; PH effect; Transthyretin

Indexed keywords

AMYLOID BETA PROTEIN; AROMATIC AMINO ACID; CATION; GLUTARALDEHYDE; HISTIDINE; IMIDAZOLINE; PHENYLALANINE; PREALBUMIN; PROTEINASE; PROTEOHEPARAN SULFATE; SCHIFF BASE; TYROSINE; PROTEIN BINDING;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; BINDING AFFINITY; CHROMATOGRAPHY; COLUMN BIOCHROMATOGRAPHY; CONTROLLED STUDY; ENTHALPY; ENZYME IMMOBILIZATION; ENZYME METABOLISM; EQUILIBRIUM DIALYSIS; HUMAN; HUMAN TISSUE; HYDROGEN BOND; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; THERMODYNAMICS; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; DRUG EFFECTS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; METABOLISM; PROCEDURES; PROTEIN CONFORMATION; PROTEIN FOLDING;

AMYLOID BETA-PEPTIDES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HEPARAN SULFATE PROTEOGLYCANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; PREALBUMIN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMODYNAMICS;

EID: 84901020686     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2014.04.021     Document Type: Article

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