Overloading and removal of N-glycosylation targets on human acetylcholinesterase: Effects on glycan composition and circulatory residence time

Biochemical Journal

Volumn 363, Issue 3, 2002, Pages 619-631

  Chitlaru, Theodor ^a   Kronman, Chanoch ^a   Velan, Baruch ^a   Shafferman, Avigdor ^a  

^a ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

Author keywords

MALDI TOF mass spectrometry; Pharmacokinetics; Protein oligomerization

Indexed keywords

CELLS; CORRELATION METHODS; ENZYMES; OPTIMIZATION; PHARMACOKINETICS;

CELL LINES;

BIOCHEMISTRY;

ACETYLCHOLINESTERASE; GLYCAN; SIALIC ACID;

ARTICLE; CELL CULTURE; CONTROLLED STUDY; DENSITY GRADIENT CENTRIFUGATION; ENZYME ACTIVITY; ESTERIFICATION; GENE OVEREXPRESSION; GLYCOSYLATION; HUMAN; HUMAN CELL; MASS SPECTROMETRY; MEAN RESIDENCE TIME; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN PROCESSING; SIALYLATION;

ACETYLCHOLINESTERASE; ANIMALS; CENTRIFUGATION, DENSITY GRADIENT; GLYCOSYLATION; HUMANS; MASS SPECTROMETRY; MICE; POLYSACCHARIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 0036565780     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3630619     Document Type: Article

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