Methods for the use of reduced affinity streptavidin

Cantor, Charles R; Sano, Takeshi

Title: Methods for the use of reduced affinity streptavidin

Patent · Mon Jan 01 00:00:00 EST 2001

OSTI ID:873629

Cantor, Charles R ^[1]; Sano, Takeshi ^[2]

Boston, MA
Waltham, MA

The present invention relates to methods for contacting biological targets using a mutated streptavidin protein having a reduced affinity for biotin.

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Research Organization:: Boston University

DOE Contract Number:: FG02-93ER61656

Assignee:: Trustees of Boston University (Boston, MA)

Patent Number(s):: US 6207390

OSTI ID:: 873629

Country of Publication:: United States

Language:: English

References (16)

A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions. Sano, T.; Glazer, A. N.; Cantor, C. R. Proceedings of the National Academy of Sciences, Vol. 89, Issue 5 https://doi.org/10.1073/pnas.89.5.1534	journal	March 1992
[2] Introduction to avidin-biotin technology Wilchek, Meir; Bayer, Edward A. Avidin-Biotin Technology https://doi.org/10.1016/0076-6879(90)84256-G	book	January 1990
Oligonucleotide Arrays: New Concepts and Possibilities Chetverin, Alexander B.; Kramer, Fred Russell Bio/Technology, Vol. 12, Issue 11 https://doi.org/10.1038/nbt1194-1093	journal	November 1994
Molecular cloning and nucleotide sequence of the streptavidin gene Argarana, Carlos E.; Kuntz, Irwin D.; Birken, Steven Nucleic Acids Research, Vol. 14, Issue 4 https://doi.org/10.1093/nar/14.4.1871	journal	January 1986
Isolation of specific lymphocyte receptors by high-performance immunoaffinity chromatography Phillips, T. M.; Frantz, S. C. Journal of Chromatography A, Vol. 444 https://doi.org/10.1016/S0021-9673(01)94004-X	journal	July 1988
Expression vectors for streptavidin-containing chimeric proteins Sano, Takeshi; Cantor, Charles R. Biochemical and Biophysical Research Communications, Vol. 176, Issue 2, p. 571-577 https://doi.org/10.1016/S0006-291X(05)80222-0	journal	April 1991
Structural origins of high-affinity biotin binding to streptavidin Weber, P.; Ohlendorf, D.; Wendoloski, J. Science, Vol. 243, Issue 4887 https://doi.org/10.1126/science.2911722	journal	January 1989
Recombinant Core Streptavidins Sano, Takeshi; Pandori, Mark W.; Chen, Xiaomin Journal of Biological Chemistry, Vol. 270, Issue 47 https://doi.org/10.1074/jbc.270.47.28204	journal	November 1995
Expression of a cloned streptavidin gene in Escherichia coli. Sano, T.; Cantor, C. R. Proceedings of the National Academy of Sciences, Vol. 87, Issue 1 https://doi.org/10.1073/pnas.87.1.142	journal	January 1990
Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. Hendrickson, W. A.; Pahler, A.; Smith, J. L. Proceedings of the National Academy of Sciences, Vol. 86, Issue 7 https://doi.org/10.1073/pnas.86.7.2190	journal	April 1989
Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Chilkoti, A.; Tan, P. H.; Stayton, P. S. Proceedings of the National Academy of Sciences, Vol. 92, Issue 5 https://doi.org/10.1073/pnas.92.5.1754	journal	February 1995
Characterization and crystallization of core streptavidin. Pähler, A.; Hendrickson, W. A.; Kolks, M. A. Journal of Biological Chemistry, Vol. 262, Issue 29 https://doi.org/10.1016/S0021-9258(18)47884-2	journal	October 1987
Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors Zoller, Mark J.; Smith, Michael Recombinant DNA Part B, p. 468-500 https://doi.org/10.1016/0076-6879(83)00074-9	book	January 1983
Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site Gitlin, G.; Bayer, E. A.; Wilchek, M. Biochemical Journal, Vol. 256, Issue 1 https://doi.org/10.1042/bj2560279	journal	November 1988
A Streptavidin Mutant Containing a Cysteine Stretch That Facilitates Production of a Variety of Specific Streptavidin Conjugates Sano, Takeshi; Smith, Cassandra L.; Cantor, Charles R. Nature Biotechnology, Vol. 11, Issue 2 https://doi.org/10.1038/nbt0293-201	journal	February 1993
Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Sano, T.; Cantor, C. R. Proceedings of the National Academy of Sciences, Vol. 92, Issue 8 https://doi.org/10.1073/pnas.92.8.3180	journal	April 1995

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mutated
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streptavidin protein
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Title: Methods for the use of reduced affinity streptavidin

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