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Titolo:
DLAD, a novel mammalian divalent cation-independent endonuclease with homology to DNase II
Autore:
Shiokawa, D; Tanuma, S;
Indirizzi:
Sci Univ Tokyo, Fac Pharmaceut Sci, Dept Biochem, Shinjuku Ku, Tokyo 1620826, Japan Sci Univ Tokyo Tokyo Japan 1620826 em, Shinjuku Ku, Tokyo 1620826, Japan Sci Univ Tokyo, Biosci Res Inst, Noda, Chiba 2780022, Japan Sci Univ Tokyo Noda Chiba Japan 2780022 Inst, Noda, Chiba 2780022, Japan
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 20, volume: 27, anno: 1999,
pagine: 4083 - 4089
SICI:
0305-1048(19991015)27:20<4083:DANMDC>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN DEOXYRIBONUCLEASE-II; APOPTOTIC RAT THYMOCYTES; CYSTIC-FIBROSIS; ACID DEOXYRIBONUCLEASES; DEPENDENT ENDONUCLEASE; MOLECULAR-CLONING; PORCINE SPLEEN; CELL-DEATH; PURIFICATION; INHIBITOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Tanuma, S Sci Univ Tokyo, Fac Pharmaceut Sci, Dept Biochem, Shinjuku Ku, 12 IchigayaFunagawara Machi, Tokyo 1620826, Japan Sci Univ Tokyo 12 IchigayaFunagawara Machi Tokyo Japan 1620826
Citazione:
D. Shiokawa e S. Tanuma, "DLAD, a novel mammalian divalent cation-independent endonuclease with homology to DNase II", NUCL ACID R, 27(20), 1999, pp. 4083-4089

Abstract

In this report, we describe the molecular cloning and characterization of DLAD, a novel mammalian deoxyribonuclease homologous to DNase II. The full length cDNA for mouse DLAD has been cloned by polymerase chain reaction, The cDNA contains a 1065 bp open reading frame (ORF) encoding a 354 amino acid protein with a calculated molecular mass of 40 767. The predicted proteinfor DLAD shares 34.4% identity with DNase II. DLAD is also homologous to three predicted proteins, C07B5.5, F09G8.2 and K04H4.6, from the nematode Caenorhabditis elegans, Furthermore, the third ORF of the fowlpox virus genome is found to encode a DLAD homologue showing 37.1% identity at the amino acid level, Northern blot analysis reveals that expression of the DLAD mRNA is highly restricted to the liver. DLAD mainly exists as a cytoplasmic protein with divalent cation-independent endonuclease activity and cleaves DNA to produce 3'-phosphoryl/5'-hydroxyl ends. It is active under a wide range of pH with maximum activity at pH 5.2, Among known DNase inhibitors tested,aurintricarboxylic acid and Zn2+ are found to be effective inhibitors of the DLAD activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 15:35:38