Results 141 to 150 of about 149,683 (183)

Evidence that ARK2N is not a core factor in transcription-coupled DNA repair. [PDF]

open access: yesProc Natl Acad Sci U S A
van Schie JJM   +2 more
europepmc   +1 more source

Identification of plasma proteins binding oxidized phospholipids using pull-down proteomics and OxLDL masking assay. [PDF]

open access: yesJ Lipid Res
Jokesch P   +7 more
europepmc   +1 more source

Structural Basis and Mechanism of a Unique Haemophore in the Haem-Iron Acquisition by Riemerella anatipestifer. [PDF]

open access: yesAdv Sci (Weinh)
Wang M   +19 more
europepmc   +1 more source

Comparative Potential of Chitinase and Chitosanase from the Strain <i>Bacillus thuringiensis</i> B-387 for the Production of Antifungal Chitosan Oligomers. [PDF]

open access: yesBioTech (Basel)
Aktuganov G   +10 more
europepmc   +1 more source

Diethylaminoethyl Sepharose (DEAE-Sepharose) microcolumn for enrichment of glycopeptides

Analytical and Bioanalytical Chemistry, 2016
N-Glycosylation is one of the most prevalent protein post-translational modifications and is involved in many biological processes, such as protein folding, cellular communications, and signaling. Alteration of N-glycosylation is closely related to the pathogenesis of diseases.
Ebtesam A Gashash   +10 more
openaire   +3 more sources

Kinetic studies of sepharose‐and CH‐sepharose‐immobilized dihydrofolate reductase

Biotechnology and Bioengineering, 1984
AbstractDihydrofolate reductase, purified to homogeneity from amethopterin‐resistant Lactobacillus casei, was immobilized by coupling to cyanogen bromide‐activated Sepharose or carbodiimide‐activated CH‐Sepharose. Coupling yields were determined by amino acid analysis following the hydrolysis of the gel. Enzyme activity was measured by the conventional
R. B. Dunlap, Faizy Ahmed
openaire   +3 more sources

Sepharose-bound trypsin and activated sepharose-bound trypsinogen

Archives of Biochemistry and Biophysics, 1974
Abstract Several enzymic and physical properties of Sepharose-bound trypsin and activated Sepharose-bound trypsinogen have been compared to those of the soluble enzyme. Sepharose-bound trypsinogen could be activated to the same extent as soluble trypsinogen; the release of the activation peptide and formation of the active site occurred as expected ...
Albert Light, Ralph J. Knights
openaire   +3 more sources

Enzyme immobilization on palmityl–sepharose

Biotechnology and Bioengineering, 1983
AbstractEnzymes adsorbed on palmityl‐substituted Sepharose 4B by hydrophobic interactions have been used in reactor‐type experiments. Results presented on immobilized glutamate dehydrogenase, trypsin, α‐chymotrypsin, and amyloglucosidase indicate possible potential of the method for continuous catalytic operations.
Mohsen Nemat-Gorgani, Khashayar Karimian
openaire   +3 more sources

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