Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry

Journal of Biological Chemistry

Volumn 280, Issue 20, 2005, Pages 19613-19624

  Bogan, Michael J ^a,b   Agnes, George R ^a   Pio, Frederic ^a   Cornell, Rosemary B ^a  

^a SIMON FRASER UNIVERSITY   (Canada)

^b LAWRENCE LIVERMORE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; ELECTROPHORESIS; ENZYMES; IMMUNOLOGY; LIPIDS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEINS; SOLUBILITY;

CAPILLARY LIQUID CHROMATOGRAPHY; CTP:PHOSPHOCHOLINE CYTIDYLYTRANSFERASE (CCT); INTERDOMAIN DISSOCIATIONS; MULTI-DOMAIN ENZYMES;

CELL MEMBRANES;

AMINO ACID; ARGININE; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; CHYMOTRYPSIN; LEUCINE; PEPTIDE; PHOSPHATIDYLCHOLINE; PROTEINASE; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CAPILLARY CHROMATOGRAPHY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHEMICAL BOND; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GEL ELECTROPHORESIS; IMMUNOBLOTTING; LIPID BILAYER; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MEMBRANE BINDING; NONHUMAN; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; IN VITRO STUDY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; PEPTIDE MAPPING; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; RAT;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE; CHYMOTRYPSIN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 21244484278     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M414028200     Document Type: Article

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