Structural elements and limited proteolysis of CD39 influence ATP diphosphohydrolase activity

Biochemistry

Volumn 38, Issue 8, 1999, Pages 2248-2258

  Schulte Am Esch II, Jan ^a   Sévigny, Jean ^a   Kaczmarek, Elzbieta ^a   Siegel, Jonathan B ^a   Imai, Masato ^a   Koziak, Katarzyna ^a   Beaudoin, Adrien R ^b   Robson, Simon C ^a,c  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITÉ DE SHERBROOKE   (Canada)

^c BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APYRASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME GLYCOSYLATION; ENZYME INACTIVATION; HUMAN; HUMAN CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROCESSING; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SPECIES DIFFERENCE; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD; APYRASE; BASE SEQUENCE; BLOTTING, WESTERN; CELLS, CULTURED; ENDOPEPTIDASES; ENDOTHELIUM, VASCULAR; ENZYME ACTIVATION; FLOW CYTOMETRY; HUMANS; HYDROLYSIS; ISOENZYMES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN ENGINEERING; SEQUENCE DELETION; SWINE; UMBILICAL VEINS;

ANIMALIA; MAMMALIA;

EID: 0000048169     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982426k     Document Type: Article

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