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Gene ; 172(2): 273-7, 1996 Jun 26.
Article in English | MEDLINE | ID: mdl-8682316

ABSTRACT

A cDNA clone coding for DNA ligase I (LigI) was isolated from a Xenopus laevis oocyte cDNA library. The 3766-bp sequence showed a putative ORF capable of encoding a 1070-amino-acid protein whose overall identity with two mammalian sequences is 63%. This identity, however, rises to 72.5% in the C-terminal portion of the protein that contains the active site. Expression of the cDNA in a prokaryotic system produces a protein that is immunologically identical to LigI and can be adenylated. The 180-kDa size of the recombinant protein is similar to the LigI detected in oocyte. Northern blot analysis of ovary and embryo RNAs revealed the expression of two (4.1 and 6 kb) LigI transcripts.


Subject(s)
DNA Ligases/genetics , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA Ligase ATP , DNA Ligases/metabolism , DNA, Complementary , Embryo, Nonmammalian/enzymology , Escherichia coli , Molecular Sequence Data , Xenopus laevis
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