Postsecretory modifications of streptavidin

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Postsecretory modifications of streptavidin.

Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: prote...

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Molecular engineering of streptavidin.

Streptavidin is a tetrameric protein produced by the bacterium Streptomyces avidinii; it has great similarity to the chicken protein avidin.14 These proteins bind the vitamin biotin with an extremely high affinity. The dissociation constant of streptavidin-biotin and avidin-biotin complexes is estimated at around M;3.4 this is one of the tightest noncovalent interactions found in biological sys...

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Hyperuricemia and increase in postsecretory reabsorption of uric acid.

M. Sanchez Bayle, Pediatric Nephrology Section, Hospital del Niño Jesus, Avda. Ménendez Pelayo, 65, E-28009 Madrid (Spain) Case 1 Case 2 Normal values1 Dear Sir, Fractional excretion of uric acid (FEUA) has been described as being derived from 4 different mechanisms: glomerular filtration, presecretory reabsorption, tubular secretion and postsecretory reabsorption [1]. Fractional excretion of u...

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Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense.

The production of antimicrobial peptides and proteins is essential for defense against infection. Many of the known human antimicrobial peptides are multifunctional, with stimulatory activities such as chemotaxis while simultaneously acting as natural antibiotics. In humans, eccrine appendages express DCD and CAMP, genes encoding proteins processed into the antimicrobial peptides dermcidin and ...

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The Crystal Structure of Monovalent Streptavidin

The strong interaction between streptavidin (SA) and biotin is widely utilized in biotechnological applications. A SA variant, monovalent SA, was developed with a single and high affinity biotin-binding site within the intact tetramer. However, its structural characterization remains undetermined. Here, we seek to determine the crystal structure of monovalent SA at 1.7-Å resolution. We show tha...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1989

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2590369