Glycosylation sites in the atrial natriuretic peptide receptor oligosaccharide structures are not required for hormone binding

European Journal of Biochemistry

Volumn 267, Issue 18, 2000, Pages 5758-5768

  Miyagi, Masaru ^a   Zhang, Xiaolun ^a   Misono, Kunio S ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

Author keywords

Glycosylation; Ligand binding; Mass spectrometry; Natriuretic peptide; Receptor

Indexed keywords

ATRIAL NATRIURETIC FACTOR; ATRIAL NATRIURETIC FACTOR RECEPTOR; GUANYLATE CYCLASE; MEMBRANE PROTEIN; OLIGOSACCHARIDE;

ANIMAL CELL; ARTICLE; BINDING KINETICS; CARBOHYDRATE ANALYSIS; GLYCOSYLATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HOMEOSTASIS; HORMONE RECEPTOR INTERACTION; LIGAND BINDING; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; CARBOHYDRATE SEQUENCE; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COS CELLS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSIDE HYDROLASES; GLYCOSYLATION; LIGANDS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; OLIGOSACCHARIDES; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, ATRIAL NATRIURETIC FACTOR; TIME FACTORS;

ANIMALIA;

EID: 0033825365     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01647.x     Document Type: Article

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16. Glycoproteins
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