Molecular Cloning of cDNA EncodingXenopus laevisDeoxyribonuclease I
| Autor: | Kouichi Mogi, Koichiro Kishi, Haruo Takeshita, Takashi Nakajima, Y Hanaoka, Toshihiro Yasuda, Osamu Hosomi, Yoshimitsu Nakashima, Shinjiro Mori |
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| Rok vydání: | 2000 |
| Předmět: |
DNA
Complementary Molecular Sequence Data Xenopus Molecular cloning Biology Transfection Biochemistry law.invention Xenopus laevis chemistry.chemical_compound Endocrinology Rapid amplification of cDNA ends law Complementary DNA Chlorocebus aethiops Genetics Animals Deoxyribonuclease I Humans Amino Acid Sequence Cloning Molecular Pancreas Molecular Biology Peptide sequence Phylogeny Base Sequence biology.organism_classification Molecular biology Recombinant Proteins Kinetics chemistry COS Cells Vertebrates Recombinant DNA DNA |
| Zdroj: | DNA Sequence. 11:247-255 |
| ISSN: | 1042-5179 |
| DOI: | 10.3109/10425170009033238 |
| Popis: | A 1200-bp cDNA encoding Xenopus laevis deoxyribonuclease I (X. laevis DNase I) was constructed from the total RNA of a X. laevis pancreas using a rapid amplification of cDNA ends method. When the cDNA was transiently transfected into COS-7 cells, the recombinant polypeptide exhibited similar enzymological properties to those of the native pancreatic DNase I. The recombinant enzyme was considerably more labile than most other vertebrate DNase I enzymes. The X. laevis DNase I polypeptide was larger than any other known vertebrate DNase I, containing a unique Cys-rich stretch of 68 or 70 amino acid residues at the carboxyl terminus, and it had less well conserved binding sites for the Ca2+, G-actin and DNA, and two DNase I signature motifs. These alterations might account for its heat instability. |
| Databáze: | OpenAIRE |
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