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Titolo:
A DNASE FROM THE TRYPANOSOMATID CRITHIDIA-FASCICULATA
Autore:
LI C; HWA KY; ENGLUND PT;
Indirizzi:
JOHNS HOPKINS UNIV,SCH MED,DEPT BIOL CHEM BALTIMORE MD 21205
Titolo Testata:
Nucleic acids research
fascicolo: 21, volume: 23, anno: 1995,
pagine: 4426 - 4433
SICI:
0305-1048(1995)23:21<4426:ADFTTC>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOCHONDRIAL-DNA; KINETOPLAST DNA; SACCHAROMYCES-CEREVISIAE; ENDONUCLEASE; PURIFICATION; SEQUENCE; NUCLEASE; REPLICATION; MINICIRCLES; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
C. Li et al., "A DNASE FROM THE TRYPANOSOMATID CRITHIDIA-FASCICULATA", Nucleic acids research, 23(21), 1995, pp. 4426-4433

Abstract

We have purified to homogeneity a DNase from a Crithidia fasciculata crude mitochondrial lysate, The enzyme is present in two forms, eitheras a 32 kDa polypeptide or as a multimer containing the 32 kDa polypeptide in association with a 56 kDa polypeptide. Native molecular weight measurements indicate that these forms are a monomer and possibly analpha(2) beta(2) tetramer, respectively, The monomeric and multimericforms of the enzyme are similar in their catalytic activities, Both digest double-stranded DNA about twice as efficiently as single-stranded DNA, They introduce single-strand breaks into a supercoiled plasmid but do not efficiently make double-strand breaks, They degrade a linearized plasmid more efficiently than a nicked plasmid, Both enzymes degrade a 5'-P-32-labeled double-stranded oligonucleotide to completion, with the 5'-terminal nucleotide ultimately being released as a 5'-mononucleotide, One difference between the monomeric and multimeric forms of the enzyme, demonstrated by a band shift assay, is that the multimeric form binds tightly to double-stranded DNA, possibly aggregating it.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 00:20:23