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Titolo:
CHARACTERIZATION AND CLONING OF TRIPEPTIDYL PEPTIDASE-II FROM THE FRUIT-FLY, DROSOPHILA-MELANOGASTER
Autore:
RENN SCP; TOMKINSON B; TAGHERT PH;
Indirizzi:
WASHINGTON UNIV,SCH MED,DEPT ANAT & NEUROBIOL ST LOUIS MO 63110 WASHINGTON UNIV,SCH MED,DEPT ANAT & NEUROBIOL ST LOUIS MO 63110 SWEDISH UNIV AGR SCI,CTR BIOMED,DEPT VET MED CHEM S-75123 UPPSALA SWEDEN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 30, volume: 273, anno: 1998,
pagine: 19173 - 19182
SICI:
0021-9258(1998)273:30<19173:CACOTP>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOCUST SCHISTOCERCA-GREGARIA; NUCLEOTIDE-SEQUENCE; MUSCA-DOMESTICA; DYE-BINDING; NEUROPEPTIDES; ENDOPEPTIDASE; PURIFICATION; SUBTILISIN; PROTEINS; CDNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
S.C.P. Renn et al., "CHARACTERIZATION AND CLONING OF TRIPEPTIDYL PEPTIDASE-II FROM THE FRUIT-FLY, DROSOPHILA-MELANOGASTER", The Journal of biological chemistry, 273(30), 1998, pp. 19173-19182

Abstract

We describe the characterization, cloning, and genetic analysis of tripeptidyl peptidase II (TPP II) from Drosophila melanogaster. Mammalian TPP II removes N-terminal tripeptides, has wide distribution, and has been identified as the cholecystokinin-degrading peptidase in rat brain. Size exclusion and ion exchange chromatography produced a 70-foldpurification; of dTPP II activity from Drosophila tissue extracts. The substrate specificity and the inhibitor sensitivity of dTPP II is comparable to that of the human enzyme. In. particular, dTPP II is sensitive to butabindide, a specific inhibitor of the rat cholecystokinin-inactivating activity. We isolated a 4309-base pair dTPP II cDNA which predicts a 1354-amino acid protein. The deduced human and Drosophila TPP II proteins display 38% overall identity. The catalytic triad, its spacing, and the sequences that surround it are highly conserved; the C-terminal end of dTPP II contains a 100-amino acid insert not found in the mammalian proteins. Recombinant dTPP II displays the predicted activity following expression in HEK cells. TPP II maps to cytological position 49F4-7; animals deficient for this interval show reduced TPP II activity.

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Documento generato il 26/09/20 alle ore 17:51:30