AVIDIN. 2. PURIFICATION AND COMPOSITION
نویسندگان
چکیده
منابع مشابه
Purification and crystallization of avidin.
An improved purification, including crystallization, of avidin from hen's-egg white is described. The product bound 15.1mug of biotin/mg, corresponding to an equivalent weight of 16200. The amino acid composition showed an integral number of amino acid residues per 16200g, which suggested that each molecule of avidin (mol. wt. approx. 66000) contained four identical subunits.
متن کاملAvidin related protein 2 shows unique structural and functional features among the avidin protein family
BACKGROUND The chicken avidin gene family consists of avidin and several avidin related genes (AVRs). Of these gene products, avidin is the best characterized and is known for its extremely high affinity for D-biotin, a property that is utilized in numerous modern life science applications. Recently, the AVR genes have been expressed as recombinant proteins, which have shown different biotin-bi...
متن کاملExpression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris.
A recombinant glycosylated avidin (recGAvi) with an acidic isoelectric point was expressed and secreted by the methylotrophic yeast Pichia pastoris. The coding sequence for recGAvi was de novo synthesized based on the codon usage of P. pastoris. RecGAvi is secreted at approximately 330mg/L of culture supernatant. RecGAvi monomer displays a molecular weight of 16.5kDa, as assessed by ESI mass sp...
متن کاملThree-dimensional structures of avidin and the avidin-biotin complex.
The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures reveal the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin. Each monomer is an eight-stranded antiparallel beta-barrel, remarkably simila...
متن کاملPurification of the subunits of transcarboxylase by affinity chromatography on avidin-sepharose.
Transcarboxylase consists of a central 12 SH subunits each of which is linked to the central subunit by two similar to 1.3 SE biotin carboxyl carrier proteins. The subunits from dissociated transcarboxylase have been difficult to isolate because conditions which stabilize them also promote their reassociation to the intact enzyme. In this paper, we describe the use of avidin-Sepharose to adsorb...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1963
ISSN: 0006-2936
DOI: 10.1042/bj0890591