Hydrolysis of synthetic substrate, L-pyroglutamyl p-nitroanilide is catalyzed solely by pyroglutamyl aminopeptidase I in rat liver cytosol

Biological and Pharmaceutical Bulletin

Volumn 26, Issue 11, 2003, Pages 1528-1533

  Abe, Koji ^a   Watanabe, Nobuaki ^a   Kosaka, Toshiyuki ^a   Yamada, Makiko ^a   Tokui, Taro ^a   Ikeda, Toshihiko ^a  

^a DAIICHI SANKYO CO   (Japan)

Author keywords

Cysteine peptidase; Cytosolic enzyme; Pyroglutamyl aminopeptidase I; Rat liver

Indexed keywords

5 OXOPROLYL PEPTIDASE; AMINO ACID; ANTIBODY; COMPLEMENTARY DNA; PEPTIDE; PROTEIN SUBUNIT; PYROGLUTAMIC ACID; PYROGLUTAMYL 3 NITROANILIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; XENOBIOTIC AGENT; NITRO DERIVATIVE;

ALKALINITY; AMINO ACID SEQUENCE; ARTICLE; CALCULATION; CHEMICAL ANALYSIS; DNA LIBRARY; ESCHERICHIA COLI; HUMAN; HYDROLYSIS; IMMUNOBLOTTING; LIVER CYTOSOL; MOLECULAR WEIGHT; NONHUMAN; PH; RAT; SEQUENCE HOMOLOGY; ANIMAL; CATALYSIS; CYTOSOL; FISCHER 344 RAT; GENETICS; LIVER; METABOLISM; MOLECULAR GENETICS; MOUSE;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CYTOSOL; HUMANS; HYDROLYSIS; LIVER; MICE; MOLECULAR SEQUENCE DATA; NITRO COMPOUNDS; PYROGLUTAMYL-PEPTIDASE I; PYRROLIDONECARBOXYLIC ACID; RATS; RATS, INBRED F344;

EID: 27844449018     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.26.1528     Document Type: Article

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