Results 1 to 10 of about 165,447 (318)

The Kinetic Mechanism of EcoRI Endonuclease [PDF]

open access: yesJournal of Biological Chemistry, 1999
Steady-state parameters governing cleavage of pBR322 DNA by EcoRI endonuclease are highly sensitive to ionic environment, with K(m) and k(cat) increasing 1,000-fold and 15-fold, respectively, when ionic strength is increased from 0.059 to 0.23 M. By contrast, pre-steady-state analysis has shown that recognition, as well as first and second strand ...
David J. Wright, W E Jack, Paul Modrich
openaire   +4 more sources

Diffusion of the Restriction Nuclease EcoRI along DNA [PDF]

open access: yesJournal of Molecular Biology, 2010
Many specific sequence DNA binding proteins locate their target sequence by first binding to DNA nonspecifically, then by linearly diffusing or hopping along DNA until either the protein dissociates from the DNA or it finds the recognition sequence. We have devised a method for measuring one-dimensional diffusion along DNA based on the ratio of the ...
Nina Y. Sidorova, Donald C. Rau
openaire   +4 more sources

Analisis 6 DNA Rekombinan dengan enzim EcoRI

open access: hybridJournal of Biological Researches, 1997
Amylase enzyme from Endomycopsis fibuligera capable to hidrolize starch into glucose. Insertion of amylase gene from Endomycopsis fibuligera into yeast (Saccharomyces cereviceae) will be able to increase the function of yeast (S.cereviceae) to digest ...
Ni Nyoman Tri Puspaningsih   +2 more
doaj   +2 more sources

Hydrogel bead-based isothermal detection (BEAD-ID) for assessing the activity of DNA-modifying enzymes [PDF]

open access: yesiScience
Summary: DNA-modifying enzymes are crucial in biological processes and have significant clinical implications. Traditional quantification methods often overlook enzymatic activity, the true determinants of enzymes’ functions.
Kathrine Nygaard Borg   +9 more
doaj   +2 more sources

Specificity of substrate recognition by the EcoRI restriction endonuclease. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1975
The substrate specificity of the EcoRI restriction endonuclease can be varied in vitro by changing the pH and the ionic environment of the reaction. Phosphodiester bond cleavage occurs at a DNA hexanucleotide sequence d(N-G-A-A-T-T-C-N)/d(N-C-T-T-A-A-G-N) when the ionic strength is high, 100 mM Tris-HCl, 50 mM NaCl, 5 mM MgCl2, and the pH is ...
Herbert W. Boyer   +5 more
openaire   +4 more sources

Peptide Inhibitor Assay for Allocating Functionally Important Accessible Sites Throughout a Protein Chain: Restriction Endonuclease EcoRI as a Model Protein System [PDF]

open access: yesBioTech
Functionally important amino acid sequences in proteins are often located at multiple sites. Three-dimensional structural analysis and site-directed mutagenesis may be performed to allocate functional sites for understanding structure‒function ...
Joji M. Otaki
doaj   +2 more sources

Sequences spanning the EcoRI substrate site [PDF]

open access: bronzeNucleic Acids Research, 1975
Substrate recognition by the EcoRI restriction endonuclease was investigated by analysis of the nucleotide sequences at the sites of enzymatic cleavage in various DNA molecules. 5'-end labeling and homochromatographic fingerprinting led to the determination of a 17-base-pair sequence spanning the EcoRI site of simian virus 40 DNA and a 15-base-pair ...
David E. Garfin   +2 more
openalex   +5 more sources

Determinants of EcoRI endonuclease sequence discrimination. [PDF]

open access: greenProceedings of the National Academy of Sciences, 1989
The arginine at position 200 of EcoRI endonuclease is thought to make two hydrogen bonds to the guanine of the sequence GAATTC and thus be an important determinant of sequence discrimination. Arg-200 was replaced by each of the other 19 naturally occurring amino acids, and the mutant endonucleases were assessed for activities in vivo and in vitro.
Michael C. Needels   +5 more
openalex   +5 more sources

Facilitated diffusion during catalysis by EcoRI endonuclease. Nonspecific interactions in EcoRI catalysis.

open access: hybridJournal of Biological Chemistry, 1985
The potential for processive EcoRI endonuclease hydrolysis has been examined on several DNA substrates containing two EcoRI sites which were embedded in identical sequence environments. With a 388-base pair circular DNA, in which the two recognition sites are separated by 51 base pairs (shorter distance) or 337 base pairs (longer distance), 77 and 34 ...
Brian Terry   +2 more
openalex   +4 more sources

Insertion mutant of bacteriophage f1 sensitive to EcoRI. [PDF]

open access: greenProceedings of the National Academy of Sciences, 1979
The nucleotide sequence A-A-T-T was inserted into the intergenic region of the f1 genome at a site cleaved by Hae III (cleavage sequence (G-G-C-C). The resultant viable phage mutant (R199) contains a single site sensitive to the restriction endonuclease EcoRI (cleavage sequence G-A-A-T-T-C). This phage is sensitive to EcoRI restriction and modification
Jef D. Boeke   +2 more
openalex   +5 more sources

Home - About - Disclaimer - Privacy