[Affinity modification of EcoRII restriction endonuclease by a DNA-duplex containing a monosubstituted pyrophosphate internucleotide bond]. 1994

Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova

Oligonucleotide duplex with an active monosubstituted pyrophosphate bond within the recognition site of the EcoRII restriction endonuclease was cross-linked to this enzyme with a yield of 10-15%. The cross-linking specificity was proved by the absence of the cross-linking to a DNA duplex with the same modification but without the EcoRII recognition site as well as by unmodified EcoRII substrate's inhibition of the cross-linking.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011756 Diphosphates Inorganic salts of phosphoric acid that contain two phosphate groups. Diphosphate,Pyrophosphate Analog,Pyrophosphates,Pyrophosphate Analogs,Analog, Pyrophosphate
D003432 Cross-Linking Reagents Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other. Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D000345 Affinity Labels Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids. Affinity Labeling Reagents,Labeling Reagents, Affinity,Labels, Affinity,Reagents, Affinity Labeling
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D015252 Deoxyribonucleases, Type II Site-Specific Enzyme systems containing a single subunit and requiring only magnesium for endonucleolytic activity. The corresponding modification methylases are separate enzymes. The systems recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition sequence to give specific double-stranded fragments with terminal 5'-phosphates. Enzymes from different microorganisms with the same specificity are called isoschizomers. EC 3.1.21.4. DNA Restriction Enzymes, Type II,DNase, Site-Specific, Type II,Restriction Endonucleases, Type II,Type II Restriction Enzymes,DNase, Site Specific, Type II,Deoxyribonucleases, Type II, Site Specific,Deoxyribonucleases, Type II, Site-Specific,Site-Specific DNase, Type II,Type II Site Specific DNase,Type II Site Specific Deoxyribonucleases,Type II Site-Specific DNase,Type II Site-Specific Deoxyribonucleases,Deoxyribonucleases, Type II Site Specific,Site Specific DNase, Type II

Related Publications

Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
May 1995, Gene,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
February 1996, FEBS letters,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
January 1984, Doklady Akademii nauk SSSR,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
January 2003, Bioorganicheskaia khimiia,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
July 1973, Nature: New biology,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
March 1989, FEBS letters,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
January 1990, Bioorganicheskaia khimiia,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
January 1986, Molekuliarnaia biologiia,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
August 2005, Biochemistry. Biokhimiia,
Z A Shabarova, and G Ia Sheflian, and S A Kuznetsova, and E A Kubareva, and O N Sysoev, and M G Ivanovskaia, and E S Gromova
January 2005, Biochemistry,
Copied contents to your clipboard!