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Biotinylated

Fig. XV-4. Schematic drawing of four streptavidin molecules bound to biotinylated lipid in a monolayer above heavy water. The scattering length density for neutron reflectivity is shown at the side. (From Ref. 30.)... Fig. XV-4. Schematic drawing of four streptavidin molecules bound to biotinylated lipid in a monolayer above heavy water. The scattering length density for neutron reflectivity is shown at the side. (From Ref. 30.)...
An enzyme-amplified detection scheme, based on tire coupling of a streptavidin-alkaline phosphatase conjugate and biotinylated target sequences was then applied. The enzyme catalysed the hydrolysis of the elecn oiiractive a-naphthyl phosphate to a-naphtlrol this product is elecU oactive and has been detected by means of differential... [Pg.15]

Atliappilly, F. K., and Hendrickson, W. A., 1995. Structure of die biotinyl domain of acetyl-CoA carboxyla.se determined by MAD phasing. Structure 3 1407. [Pg.850]

Biotinyl diazirine photophore for probing receptor-ligand 98H(47)625. [Pg.230]

Stults, N. L., et al. (1992). Use of recombinant biotinylated aequorin in microtiter and membrane-based assays Purification of recombinant aequorin from Escherichia coli. Biochemistry 31 1433-1442. [Pg.441]

Biotin can be synthesized by the human colon flora. The question to which extent this production contributes to covering the host-organism s requirements is, however, subject to discussion. In most foods of animal origin as well as in cereals, biotin prevails in the protein (= enzyme)-bound form as e-N-biotinyl-L-lysine (= biocytin). Brewer s yeast, liver, soya beans, and peanuts number among the biotin rich foods [1]. [Pg.270]

These examples are part of a broader design scheme to combine catalytic metal complexes with a protein as chiral scaffold to obtain a hybrid catalyst combining the catalytic potential of the metal complex with the enantioselectivity and evolvability of the protein host [11]. One of the first examples of such systems combined a biotinylated rhodium complex with avidin to obtain an enantioselective hydrogenation catalyst [28]. Most significantly, it has been shovm that mutation-based improvements of enantioselectivity are possible in these hybrid catalysts as for enzymes (Figure 3.7) [29]. [Pg.70]

Fig. 35 TEM image of peptide fibres coated with streptavidin-gold nanoparticles, (a, b) Peptides with biotin directly attached (using SAF-pl-biotin) particles are 10 nm, (c) Peptide fibre with biotinylated anti-FLAG antibody attached that was then bound to gold-labelled streptavidin particles are 5 nm. Reprinted with permission from Ryadnov and Woolfson [76]. Copyright 2004 American Chemical Society... Fig. 35 TEM image of peptide fibres coated with streptavidin-gold nanoparticles, (a, b) Peptides with biotin directly attached (using SAF-pl-biotin) particles are 10 nm, (c) Peptide fibre with biotinylated anti-FLAG antibody attached that was then bound to gold-labelled streptavidin particles are 5 nm. Reprinted with permission from Ryadnov and Woolfson [76]. Copyright 2004 American Chemical Society...
FIG. 6 Successive coupling of two different biotinylated compounds with the DNA-STV conjugates 2 [33]. In a first step, a macromolecular functional component (FC, represented by the shaded ellipse), such as a biotinylated enzyme or oligonucleotide, is coupled. In a second step, a biotinylated low-molecular-weight modulator M, represented by the shaded sphere) is coupled to the remaining free biotin-binding sites. The modulator is used to modify the conjugate s hybridization properties or to supplement its functionality. [Pg.399]

FIG. 8 Synthesis of oligomeric DNA-STV conjugates 7 from 5, 5 -bis-biotinylated DNA and STV [49]. Note that the schematic structure of 7 is simplified, since a portion of the STV molecules function as tri- and tetravalent linker molecules between adjacent DNA fragments. [Pg.402]

Streptavidin-single-stranded DNA covalent conjugates were described as the building blocks for assembling nanostructured scaffolds [31], The amount and type of biotinylated ligands were used to modulate the affinity of duplex formation between solid-phase-bound nucleic acid templates and DNA-streptavidin conjugates. This system has been proposed for the design of fine-tuned sequence detection systems. [Pg.434]

Patterning of enzyme monolayers on a solid surface was carried out by photoactivation of immobilized monolayer of caged -biotin derivatives in selected areas. Specific oriented binding of enzyme-avidin conjugates could be readily made to the photoactivated zones [42]. Oriented immobilization of G-protein-coupled receptors on a solid surface was also made possible on a biotinylated surface by first immobilizing streptavidin, followed by the immobilization of biotinylated G-protein-coupled receptor [43]. [Pg.465]

Another alternative prototype of memory array, consisting of data stored as electrostatic charge or molecular dipole in a two-dimensional network of streptavidin cross-linked by biotinylated porphyrin derivative, was also suggested. Information reading was expected to be carried out using the electric force mode of the atomic force microscope [70]. [Pg.469]

Biotin also has a role in regulation of the cell cycle, acting to biotinylate key nuclear proteins. [Pg.495]

To check if PemB is surface exposed, E. chrysanthemi cells were subjected to proteolysis. Treatment of the cell suspension with trypsin, proteinase K or chimotrypsin at a concentration of 0.1 to 1 mg/ml for 1 h did not cause PemB proteolysis or its liberation into the medium. Cell pre-treatment with EDTA-lysozyme, which renders the periplasmic proteins accessible to proteases, gave no effect. PemB was also resistant to proteolytic digestion in extract of cells disrupted by sonication or in a French press. Only addition of Triton X-100 (up to 0.1%) causing formation of the micelles with PemB lead to a quick proteolyis of this protein (data not shown). In another approach to analyse the PemB exposition, bacterial cells were labelled with sulfo-NHS-biotin. This compound is unable to cross membranes and biotinylation... [Pg.839]


See other pages where Biotinylated is mentioned: [Pg.266]    [Pg.542]    [Pg.28]    [Pg.516]    [Pg.516]    [Pg.516]    [Pg.516]    [Pg.154]    [Pg.63]    [Pg.65]    [Pg.39]    [Pg.352]    [Pg.352]    [Pg.353]    [Pg.353]    [Pg.372]    [Pg.379]    [Pg.397]    [Pg.398]    [Pg.399]    [Pg.399]    [Pg.400]    [Pg.401]    [Pg.402]    [Pg.402]    [Pg.407]    [Pg.415]    [Pg.415]    [Pg.428]    [Pg.465]    [Pg.465]    [Pg.494]    [Pg.495]    [Pg.341]    [Pg.840]    [Pg.841]   
See also in sourсe #XX -- [ Pg.573 ]

See also in sourсe #XX -- [ Pg.12 , Pg.58 , Pg.106 , Pg.120 , Pg.149 ]

See also in sourсe #XX -- [ Pg.573 ]

See also in sourсe #XX -- [ Pg.18 ]




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Affinity biotinylation approach

Affinity chromatography biotinylated

Affinity chromatography using biotinylated chromatographic probes

Amine-Reactive Biotinylation Agents

Amplicon biotinylated

Antibodies biotinylated

Antibodies biotinylated, preparation

Antibodies biotinylation

Antigens biotinylated antibodies

Aryl azides in biotinylation reagents

Avidin biotinylated

Avidin biotinylated phospholipids

Avidin complex with biotinylated

Background biotinylated probes

Binding of biotinylated protein or RNA to streptavidin beads

Biotin biotinylated antibody

Biotin biotinylated peptide

Biotin biotinylated protein

Biotinyl

Biotinyl esters

Biotinyl hydrazides

Biotinyl transferase activity

Biotinyl- 6-aminoquinoline

Biotinyl-L-3-(2-naphthyl)-alanine hydrazide

Biotinylated Aminopyridine

Biotinylated FAB

Biotinylated PCR products

Biotinylated RNA

Biotinylated antibodies, mixture

Biotinylated aptamer

Biotinylated bovine serum albumin

Biotinylated conjugate

Biotinylated fluorescein

Biotinylated gastrin

Biotinylated glucose oxidase

Biotinylated glycopolymer

Biotinylated immunoglobulins

Biotinylated interface, design

Biotinylated lipid conjugates

Biotinylated liposomes, binding

Biotinylated molecules

Biotinylated nucleic acid

Biotinylated nucleic acid development

Biotinylated oligonucleotides

Biotinylated peptides

Biotinylated probes

Biotinylated probes detection

Biotinylated probes purification

Biotinylated protein layer

Biotinylated serum albumins

Biotinylated target

Biotinylated tyramine

Biotinylation

Biotinylation Reagents Containing Discrete PEG Linkers

Biotinylation approach

Biotinylation biotin targeting assay

Biotinylation cell surface

Biotinylation compounds

Biotinylation compounds containing

Biotinylation conjugation properties

Biotinylation dendrimers

Biotinylation determining level

Biotinylation enzymes

Biotinylation extraction

Biotinylation fluorescent derivatives

Biotinylation glycans

Biotinylation interactions

Biotinylation level

Biotinylation liposomes

Biotinylation of Amine-Dendrimers

Biotinylation of Histones

Biotinylation of Oligonucleotides

Biotinylation of antigen

Biotinylation of immunoreactants

Biotinylation of proteins

Biotinylation reagent preparation

Biotinylation reagents

Biotinylation reagents amine reactive

Biotinylation reagents basic design

Biotinylation reagents cleavable

Biotinylation reagents importance of spacer arm

Biotinylation reagents length

Biotinylation reagents photoreactive

Biotinylation reagents techniques

Biotinylation techniques

Biotinylation use in avidin/streptavidin

Biotinylation using

Biotinylation, heparin

Biotinylation, histones

Biotinylation, monoclonal antibody

Biotinylation, target hapten

Carbohydrate antigens biotinylation

Carboxyl-Reactive Biotinylation Agents

Carboxylases biotinylation

Chemokine biotinylated

Chemokine biotinylation

Cysteine biotinylation

Cysteine residue, biotinylation

DNA, biotinylated

Dendrimer biotinylation

E-N-Biotinyl-L-lysine,

Enzyme-linked biotinylated

Enzyme-linked immunosorbent biotinylated

Enzymes biotinylated

Firefly, luciferase, biotinylated

Glycan biotinylation reagents

Glycoproteins biotinylation

Haptens target, biotinylation

Holocarboxylase synthetase histone biotinylation

Hydrazide biotinylation reagents

Hydrazides biotinylation reagents

Immunoglobulin binding biotinylated

Immunoglobulins biotinylation

Insulin biotinylation

Interaction with biotinylated antibodies

Interaction with biotinylated liposomes

Iodoacetyl in biotinylation reagents

Level of Biotinylation

Lipoproteins biotinylated

Liposomes biotinylated

Maleimide biotinylation reagents

Modification biotinylation reagents

Oligonucleotide probes biotinylated

Oligosaccharides biotinylation

Phospholipids biotinylated

Plasma membrane biotinylation

Preparation of Biotinylated Enzymes

Preparation of Biotinylated or Avidin-Conjugated Liposomes

Protein biotinylated

Proteins biotinylation

Selections using biotinylated antigen

Streptavidin biotinylated antibodies

Subject biotinylation

Sulfhydryl-Reactive Biotinylation Agents

Sulfhydryls biotinylation

Surface Biotinylation-Tight Junction Permeability Assay

Tumor biotinylated antibodies

Tyramide biotinylated

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