Effect of mutations of N- and C-terminal charged residues on the activity of LCAT

Journal of Lipid Research

Volumn 42, Issue 4, 2001, Pages 471-479

  Peelman, F ^a   Vanloo, B ^a   Verschelde, J L ^a   Labeur, C ^a   Caster, H ^a   Taveirne, J ^a   Verhee, A ^a   Duverger, N ^a   Vandekerckhove, J ^a   Tavernier, J ^a   Rosseneu, M ^a  

^a Lab for Lipoprotein Chemistry   (Belgium)

Author keywords

Enzyme; Ionic interactions; Lipase; Lipoproteins; Phospholipid; Structure

Indexed keywords

HIGH DENSITY LIPOPROTEIN; HYDROLASE; LIPOPROTEIN; LOW DENSITY LIPOPROTEIN; PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE; PHOSPHOLIPID; TRIACYLGLYCEROL LIPASE;

ACYLATION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL STRAIN COS1; CHEMICAL BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; COS CELLS; HUMANS; LIPASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLCHOLINE-STEROL O-ACYLTRANSFERASE; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 0035061354     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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