Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23

Journal of Biological Chemistry

Volumn 278, Issue 33, 2003, Pages 30469-30477

  Fourie, Anne M ^a   Coles, Fawn ^a   Moreno, Veronica ^a   Karlsson, Lars ^a  

^a JOHNSON AND JOHNSON PHARMACEUTICAL RESEARCH AND DEVELOPMENT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CYTOLOGY; NITROGEN COMPOUNDS; PROTEINS; TISSUE; TUMORS;

BIOLOGICAL ACTIVITY;

BIOCHEMISTRY;

ADAM 15 PROTEINASE; ADAM 28 PROTEINASE; ADAM 8 PROTEINASE; CD23 ANTIGEN; COMPLEMENTARY DNA; DISINTEGRIN; MDCL PROTEIN; METALLOPROTEINASE; RECOMBINANT PROTEIN; SYNTHETIC PEPTIDE; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG;

ALLERGY; ANIMAL CELL; ARTICLE; B LYMPHOCYTE; CATALYSIS; ENZYME ACTIVITY; ENZYME SUBSTRATE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; INFLAMMATION; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ADAM PROTEINS; ANTIGENS, CD; B-LYMPHOCYTES; CELL LINE; ENZYME INHIBITORS; HUMANS; HYPERSENSITIVITY; KIDNEY; MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, IGE; SOLUBILITY; SUBSTRATE SPECIFICITY; TRANSFECTION;

ANIMALIA;

EID: 0042232590     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M213157200     Document Type: Article

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