Results 231 to 240 of about 49,644 (261)
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Biotinylated Stealth® magnetoliposomes
Chemistry and Physics of Lipids, 2002Dimyristoylphosphatidylethanolamine (DC(14:0)PE) and the dioleoyl analogue (DC(18:1cis)PE) were mixed with alpha-biotinylamido-omega-N-succinimidoxycarbonyl-poly(ethylene glycol) (NHS-PEG-biotin) and quantitatively converted to alpha-biotinylamido-omega-(dimyristoylphosphatidylethanolamino-carbonyl)polyethylene glycol (DC(14:0)PE-PEG-biotin) and the ...
Michael, Hodenius +5 more
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Biotinylated gene therapy vectors
Expert Opinion on Biological Therapy, 2003The avidin-biotin system is a fundamental technology in biomedicine for immunolocalisation, imaging, nucleic acid blotting and protein labelling. This technology has recently been adapted for use in gene therapy vector applications to add proteins or cell-targeting ligands to non-viral and viral vectors. Two biotinylation technologies are being used in
Michael A, Barry +6 more
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Current Protocols in Protein Science, 2010
AbstractSince its discovery in the first half of the twentieth century, the high‐affinity, noncovalent interaction between biotin (vitamin H) and the avian protein avidin (and its bacterial homologs) has been exploited for many diverse biotechnology applications.
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AbstractSince its discovery in the first half of the twentieth century, the high‐affinity, noncovalent interaction between biotin (vitamin H) and the avian protein avidin (and its bacterial homologs) has been exploited for many diverse biotechnology applications.
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International Journal of Peptide and Protein Research, 1992
We have developed an expeditious method for the incorporation of the biotinylaminocaproyl moiety on the ε‐amino group of a lysine residue within a peptide chain in a site‐specific manner. Using t‐Boc chemistry for the solid phase synthesis approach and a base labile, acid stable protecting group (Fmoc‐) for the ε‐amino group of the target lysine, we ...
SESHA NATARAJAN +5 more
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We have developed an expeditious method for the incorporation of the biotinylaminocaproyl moiety on the ε‐amino group of a lysine residue within a peptide chain in a site‐specific manner. Using t‐Boc chemistry for the solid phase synthesis approach and a base labile, acid stable protecting group (Fmoc‐) for the ε‐amino group of the target lysine, we ...
SESHA NATARAJAN +5 more
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Fragmentation of biotinylated cyclic peptides
Rapid Communications in Mass Spectrometry, 2004Abstract Electrospray ionization coupled with tandem mass spectrometry (MS/MS) was used to determine the preferred binding site(s) of biotin NHS ester with a series of cyclic peptides with antibiotic properties.
Michael E, Lassman +2 more
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2014
Biotin is a naturally occurring vitamin that binds with high affinity to avidin and streptavidin proteins. Because biotin is small (244 Da), it can be conjugated to many proteins without altering their biological activities. The biotinylated molecule can be detected in ELISA, dot blot, or Western blot methods (see Western Blotting using ...
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Biotin is a naturally occurring vitamin that binds with high affinity to avidin and streptavidin proteins. Because biotin is small (244 Da), it can be conjugated to many proteins without altering their biological activities. The biotinylated molecule can be detected in ELISA, dot blot, or Western blot methods (see Western Blotting using ...
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1994
Using the characteristic of a high-affinity complex between avidin and biotin, biotinylated antibodies have wide applications in various immunochemical assays, especially where signal amplification is required. A method is described here for the biotinylation of immunoglobulins.
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Using the characteristic of a high-affinity complex between avidin and biotin, biotinylated antibodies have wide applications in various immunochemical assays, especially where signal amplification is required. A method is described here for the biotinylation of immunoglobulins.
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1990
Publisher Summary This chapter discusses the procedures by which researchers have incorporated biotin moieties into proteins. Several laboratories have reported the use of an avidin-based assay for detecting the extent of biotinylation. An effective method for detecting the average number of biotin groups per protein molecule would be to first remove
Edward A. Bayer, Meir Wilchek
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Publisher Summary This chapter discusses the procedures by which researchers have incorporated biotin moieties into proteins. Several laboratories have reported the use of an avidin-based assay for detecting the extent of biotinylation. An effective method for detecting the average number of biotin groups per protein molecule would be to first remove
Edward A. Bayer, Meir Wilchek
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In vivo enzymatic protein biotinylation
Biomolecular Engineering, 1999Biotin is biologically active only when protein-bound and is covalently attached to a class of important metabolic enzymes, the biotin carboxylases and decarboxylases. Biotinylation is a relatively rare modification, with between one and five biotinylated protein species found in different organisms.
A, Chapman-Smith, J E, Cronan
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Biotinylation modifies red cell antigens
Transfusion, 1999BACKGROUND: Chemical biotinylation of red cell membranes may be useful for several clinical applications, including red cell survival studies.STUDY DESIGN AND METHODS: To examine the possible effects of biotinylation on red cell antigens, standard hemagglutination assays were performed on matched sets of control and biotinylated red cells.
H, Cowley +5 more
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