NeutrAvidin
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Neutralite Avidin protein is a de
affinity is retained because the carbohydrate is not necessary for this activity. Avidin has a high pI but NeutrAvidin has a near-neutral pI (pH 6.3), minimizing non-specific interactions with the negatively-charged cell surface or with DNA/RNA. Neutravidin still has lysine residues that remain available for derivatization or conjugation
.
Like avidin itself, NeutrAvidin is a
biochemical applications, streptavidin
, which also binds very tightly to biotin, may be used interchangeably with NeutrAvidin.
Avidin immobilized onto solid supports is also used as purification media to capture
cell surface proteins can be specifically labelled with membrane-impermeable biotin reagent
, then specifically captured using a NeutrAvidin support.
References
- Bayer, Ed: "The avidin-biotin system", Dept. of Biological Chemistry, Weizmann Institute of Science, Israel
- Y. Hiller, J.M. Gershoni, E. A. Bayer, M. Wilchek (1987), "Biotin binding to avidin. Oligosaccharide side chain not required for ligand association", )
- Edward A. Bayer, Fabien De Meester, Tikva Kulik, Meir Wilchek (1995), "Preparation of deglycosylated egg white avidin", Applied Biochemistry and Biotechnology, vol. 53, no. 1, pp. 1–9, doi:10.1007/BF02783477)
{{citation}}: CS1 maint: multiple names: authors list (link - Ari T. Marttila, Olli H. Laitinen, Kari J. Airenne, Tikva Kulik, Edward A. Bayer, Meir Wilchek, Markku S. Kulomaa (2000), "Recombinant NeutraLite Avidin: a non‐glycosylated, acidic mutant of chicken avidin that exhibits high affinity for biotin and low non‐specific binding properties", FEBS Letters, vol. 467, no. 1, pp. 31–36, doi:10.1016/S0014-5793(00)01119-4)
{{citation}}: CS1 maint: multiple names: authors list (link
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