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Chicken avidin exhibits pseudo-catalytic properties. Biochemical, structural, and electrostatic consequencesStructure of Bradavidin – C-Terminal Residues Act as Intrinsic LigandsSupported bilayer electrophoresis under controlled buffer conditions.Development of a streptavidin-conjugated single-chain antibody that binds Bacillus cereus sporesThermal and sodium dodecylsulfate induced transitions of streptavidinIntersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidinStructural characterization of core-bradavidin in complex with biotin.A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions.Expression of a cloned streptavidin gene in Escherichia coli.A Novel Streptavidin-luciferase Fusion Protein: Preparation, Properties and Application in Hybridization Analysis of DNA.Preparation and functional evaluation of RGD-modified streptavidin targeting to integrin-expressing melanoma cells.Complexes of streptavidin-fused antigens with biotinylated antibodies targeting receptors on dendritic cell surface: a novel tool for induction of specific T-cell immune responses.Flow cytometric detection of progastrin interaction with gastrointestinal cells.Mutations for decreasing the immunogenicity and maintaining the function of core streptavidin.Studies on the biotin-binding site of avidin. Minimized fragments that bind biotin.Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli.Signal peptide does not inhibit binding of biotin to streptavidin.Tissue distribution of avidin and streptavidin injected to mice. Effect of avidin carbohydrate, streptavidin truncation and exogenous biotin.Streptavidin-coated surfaces suppress bacterial colonization by inhibiting non-specific protein adsorption.Purification of CD47-streptavidin fusion protein from bacterial lysate using biotin-agarose affinity chromatography.GAP promoter-based fed-batch production of highly bioactive core streptavidin by Pichia pastoris.Production of Recombinant Streptavidin and Optimization of Refolding Conditions for Recovery of Biological Activity.IgG-detection devices for the Tus-Ter-lock immuno-PCR diagnostic platform.
P2860
Q27632382-23405A77-93BB-49A7-921E-E64A5EF31F96Q27679001-AB196271-A6DF-4C38-951C-10166D5249A4Q30469562-28C16900-5D84-4ABC-BBAB-5874691745BCQ33715035-C0D8BD04-F406-487B-8FAD-E1AB7A6AEAC7Q34187381-5FF7A31F-2CE8-4151-8548-EF12C359F0F5Q34420433-2F33EDB8-E04F-4B66-8091-5F4B26FFA5EAQ36352176-D8A61FF2-9EA2-4366-9835-B9B9A788830DQ36846021-6F8E78B2-0BDD-4438-9F83-C3277EDD1811Q37660396-912AA44A-D76C-4FCC-929A-92848DC4EBF3Q38290134-0C3B7982-08FF-46A7-B144-9B9CB9A26A6FQ39242833-56AF30B1-DC49-41A8-933E-B059E3E7C052Q39456671-10907FE0-847C-4854-BA6B-3BAE407DEC3BQ39954950-E82C16D4-5979-4DCD-B843-0D45A606EAA8Q41583623-B8CA9BE2-4026-4682-9901-9C36176EE7C1Q42126577-A550EFDF-5162-4A8B-986F-B5F29D6CA7C1Q42808844-BC083662-DBEF-4591-B3F4-45CF06AE66FEQ46678725-F37BF5E3-6CCF-4070-8272-429039DFD8F7Q46792433-49F36899-063F-4F16-8139-141801C43A96Q47621301-F1251C17-71F3-4BC4-A2DB-F909EB0B6B92Q47816658-B25C3D73-10F3-4617-8239-9DA11777D8E2Q47822655-DF2C5C44-CD2E-45D7-A4F8-1001B9792EDBQ54202179-DF324FCB-CDCC-42C6-ADD6-789528247A7CQ54344816-E310B75D-E67F-41F2-B134-A05B98EFA028
P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Postsecretory modifications of streptavidin.
@en
Postsecretory modifications of streptavidin.
@nl
type
label
Postsecretory modifications of streptavidin.
@en
Postsecretory modifications of streptavidin.
@nl
prefLabel
Postsecretory modifications of streptavidin.
@en
Postsecretory modifications of streptavidin.
@nl
P2093
P2860
P356
P1433
P1476
Postsecretory modifications of streptavidin.
@en
P2093
P2860
P304
P356
10.1042/BJ2590369
P407
P577
1989-04-01T00:00:00Z