Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography.
about
A modified IMAC method for the capture of target protein from mammalian cell culture harvest containing metal chelating species.Use of immobilized metal ions as a negative adsorbent for purification of enzymes: application to phosphoglycerate mutase from chicken muscle extract and horseradish peroxidase.Applications of novel affinity cassette methods: use of peptide fusion handles for the purification of recombinant proteins.Copper: from neurotransmission to neuroproteostasisNanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides.An unusual metal-binding cluster found exclusively in the avian breast muscle troponin T of Galliformes and Craciformes.Spontaneous conversion of PrPC to PrPSc.Involvement of Histidine Residue His382 in pH Regulation of MCT4 Activity.N-terminal processing of affinity-tagged recombinant proteins purified by IMAC procedures.Purification and properties of the cellular prion protein from Syrian hamster brain.Application of immobilized metal affinity chromatography in proteomics.Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases.New developments in protein isolation, purification, and characterization.Layer-by-layer assembly of thick, Cu(2+)-chelating filmsSelective Removal of Hemoglobin from Blood Using Hierarchical Copper Shells Anchored to Magnetic Nanoparticles.Immobilized metal ion affinity chromatography: a review on its applications.Interaction of calreticulin with protein disulfide isomerase.Overproduction of Thermus sp. Strain T2 beta-galactosidase in Escherichia coli and preparation by using tailor-made metal chelate supports.Purification of Rhizobium leguminosarum HypB, a nickel-binding protein required for hydrogenase synthesis.Engineering metal binding sites into recombinant proteins for facile purification.Electrothermal supercharging of proteins in native MS: effects of protein isoelectric point, buffer, and nanoESI-emitter tip size.Novel zinc-binding site in the E2 domain regulates amyloid precursor-like protein 1 (APLP1) oligomerization.Surface topography of histidine residues of tetanus toxin probed by immobilized-metal-ion affinity chromatography.Detection of ubiquityl-calmodulin conjugates with a novel high-molecular weight ubiquitylprotein-isopeptidase in rabbit tissues.Methacryloylamidoglutamic acid having porous magnetic beads as a stationary phase in metal chelate affinity chromatography.Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins.One-step purification, covalent immobilization, and additional stabilization of poly-His-tagged proteins using novel heterofunctional chelate-epoxy supports.Molecular simulations to determine the chelating mechanisms of various metal ions to the His-tag motif: a preliminary study.Immobilized metal affinity beads for ferritin adsorption.IMAC: nonlinear elution chromatography of proteins.Removal of cleavage slow points from affinity tags used in the IMAC purification of recombinant proteins.DNA-Templated Introduction of an Aldehyde Handle in Proteins.Importance of the Support Properties for Immobilization or Purification of Enzymes
P2860
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P2860
Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography.
description
1989 nî lūn-bûn
@nan
1989 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի մարտին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Surface topography of histidin ...... l ion affinity chromatography.
@en
type
label
Surface topography of histidin ...... l ion affinity chromatography.
@en
prefLabel
Surface topography of histidin ...... l ion affinity chromatography.
@en
P2093
P2860
P356
P1476
Surface topography of histidin ...... l ion affinity chromatography.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.6.1811
P407
P577
1989-03-01T00:00:00Z