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"Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation." |
Suzuki H, Uchida K, Shima H, Sato T, Okamoto T, Kimura T, Miwa M |
Published July 31, 1987 in Biochem Biophys Res Commun volume 146 .
Pubmed ID: 3113420
Abstract:
| Human placental poly(ADP-ribose) polymerase was purified and the NH2-terminal amino acid sequences of 16 KDa and 40 KDa chymotryptic peptides were determined. Screening of a lambda gt11 cDNA library of normal human placenta with a 51-mer oligodeoxyribonucleotide yielded one clone with a 1.8 Kb insert and two clones with 2.1 Kb inserts. The amino acid sequence deduced from the nucleotide sequence of the 1.8 Kb insert exactly matched the determined amino acid sequences. From a Northern blot analysis, a single 3.6 Kb mRNA was detected in HL-60 cells. Furthermore, the RNA expression of the poly(ADP-ribose) polymerase gene was shown to decrease during the granulocytic differentiation of HL-60 cells upon induction by retinoic acid. |
This publication refers to following REPAIRtoire entries:
| Proteins |
Last modification of this entry: Oct. 6, 2010
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