Polymorphic forms of human ADP-ribosyltransferase-1: Differences in their catalytic activities revealed by labeling of membrane-associated substrates

European Journal of Biochemistry

Volumn 262, Issue 2, 1999, Pages 342-348

  Yadollahi Farsani, Masoud ^a   Kefalas, Panagiotis ^a   Saxty, Barbara A ^a   MacDermot, John ^a  

^a IMPERIAL COLLEGE SCHOOL OF MEDICINE   (United Kingdom)

Author keywords

ADP ribosyltransferase 1; Gene expression; Polymorphism

Indexed keywords

COMPLEMENTARY DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

ALLELE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME POLYMORPHISM; ENZYME SUBSTRATE; HUMAN; HUMAN EXPERIMENT; NONHUMAN; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; STEREOCHEMISTRY;

ANIMALS; BASE SEQUENCE; CATALYSIS; CELL LINE; CELL MEMBRANE; CLONING, MOLECULAR; CRICETINAE; CRICETULUS; DNA PRIMERS; FIBROBLAST GROWTH FACTOR 2; HUMANS; MUTAGENESIS, SITE-DIRECTED; PHOSPHATIDYLINOSITOL DIACYLGLYCEROL-LYASE; PHOSPHOLIPASE C; POLY(ADP-RIBOSE) POLYMERASES; POLYMORPHISM, RESTRICTION FRAGMENT LENGTH; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 0033152765     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00368.x     Document Type: Article

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