PMID: 8960102Nov 29, 1996Paper

Biotinylation of proteins via amino groups can induce binding to U937 cells, HL-60 cells, monocytes and granulocytes

Journal of Immunological Methods
D StormM Kaul

Abstract

The use of biotinylated ligands for the flow cytometric detection of cell surface receptors has become a popular alternative to radioreceptor assays. Although the biotinylation of a protein is a relatively mild chemical reaction several reports have mentioned the fact that the number and location of biotin moieties coupled to amino groups of a protein can alter its physicochemical properties and impair biological activity. In the present study we show for a variety of biotinylated functionally unaltered ligands that biotinylation by N-hydroxysuccinimide (NHS) esters of biotin can induce a binding to cell surfaces, which is not specific for the respective unlabelled ligand. C1q, C1 inhibitor (C1-INH), alpha 1-antitrypsin (AT), ovalbumin (OV), transferrin and soybean trypsin inhibitor (STI) were labelled with S-NHS-LC-biotin and activated C1s (C1s) with NHS-biotin. Biotinylation of C1q, C1s and C1-INH exerted negligible effects on biological function, antigenicity or electrophoretic mobility but when labelled and unlabelled proteins were assayed for binding to monocytic U937 cells, promyelocytic HL-60 cells, monocytes and granulocytes, a remarkable binding was observed for biotinylated C1q, C1-INH and C1s. In contrast, no binding...Continue Reading

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Citations

Oct 24, 2007·Protein Expression and Purification·Xiaolin SunTaha Al-Samarrai
Oct 26, 2005·Biochemical and Biophysical Research Communications·Yufeng TaoFumito Tani
Jul 15, 2015·Canadian Journal of Physiology and Pharmacology·Toshinobu Kuroishi
Jan 12, 1999·Analytical Biochemistry·O E GalaninaN V Bovin
Aug 19, 2006·Biotechnology and Bioengineering·Anthony Sang Won HamMichael B Lawrence
Nov 5, 1997·Immunity·L B KlicksteinA Nicholson-Weller
Jun 8, 2001·The Journal of Immunology : Official Journal of the American Association of Immunologists·M A Dragon-DureyW H Fridman

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