Results 241 to 250 of about 169,356 (299)

Investigation of a cryptic ligand binding site on Plasmodium falciparum Hsp90. [PDF]

open access: yesBioorg Med Chem
Mansfield CR   +3 more
europepmc   +1 more source

ELAVL1 and ELAVL4 Are Required for Musashi-Dependent Translational Activation. [PDF]

open access: yesBiomolecules
Bronson K   +9 more
europepmc   +1 more source

The E. coli DnaX clamp loader sharply bends DNA to load β-clamp at nicks and small gaps. [PDF]

open access: yesMol Cell
Zheng F   +5 more
europepmc   +1 more source

Structure of human cytoplasmic Pol II complex explains global transcription repression by GDOWN1. [PDF]

open access: yesNat Commun
Schmitzová J   +8 more
europepmc   +1 more source
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Fractionation of Soluble Proteins Using DEAE-Sepharose, SP-Sepharose, and Phenyl Sepharose Chromatographies for Proteomics

Methods in Molecular Biology, 2017
In order to simplify a complex mixture of soluble proteins from tissues, a protocol to fractionate samples prior to two-dimensional (2D) gel electrophoresis has been developed. These methods involve the use of DEAE-Sepharose, SP-Sepharose, and phenyl Sepharose chromatographic columns and the fractionation of the protein mixtures based on differential ...
Tara Sigdel
exaly   +3 more sources

Sepharose‐C3

Scandinavian Journal of Immunology, 1976
Summary. Effective conditions were devised for the specific depletion from lymphocyte populations of complement receptor lymphocytes (CRL) on columns of Sepharose‐C3. CRL among both human and murine lymphocytes were found by this method to be a subpopulation of B cells.
M. B. PEPYS, A. J. BELL, I. F. ROWE
openaire   +2 more sources

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.
He, Zhu   +10 more
openaire   +2 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
F, Ahmed, R B, Dunlap
openaire   +2 more sources

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