Selective binding of mouse estradiol.receptor complexes to oligo(dT)-cellulose
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چکیده
منابع مشابه
BINDING OF THE ANTITUMOR DRUG ADRIAMYCIN TO DNA-HISTONE COMPLEXES
Isotherms of the binding of the anthracycIine antibiotic, adriamycin (adriblastin), to DNA histone complexes was studied by means of spectroscopic analysis. The results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with DNA, (b) binding of the drug to DNA did not change the binding affinity of histone to DNA and, (c) in the explored binding range...
متن کاملbinding of the antitumor drug adriamycin to dna-histone complexes
isotherms of the binding of the anthracyciine antibiotic, adriamycin (adriblastin), to dna histone complexes was studied by means of spectroscopic analysis. the results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with dna, (b) binding of the drug to dna did not change the binding affinity of histone to dna and, (c) in the explored binding range of r
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The interaction between cellulase enzymes and their substrates is of central importance to several technological and scientific challenges. Here we report that the binding of cellulose binding modules (CBM) from Trichoderma reesei cellulases Cel6A and Cel7A show a major difference in how they interact with substrates originating from wood compared to bacterial cellulose. We found that the CBM f...
متن کاملStudies on the cellulose-binding domains adsorption to cellulose.
Cellulose-binding domains (CBD) are modular peptides, present in many glycanases, which anchor these enzymes to the substrate. In this work, the effect of CBD adsorption on the surface properties of a model cellulose, Whatman CF11, was studied. The methods applied include inverse gas chromatography (IGC), ESCA, X-ray diffraction, and scanning electron microscopy (SEM). The CBD partition affinit...
متن کاملCharacterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A.
Cellulose-binding protein A (CbpA), a component of the cellulase complex of Clostridium cellulovorans, contains a unique sequence which has been demonstrated to be a cellulose-binding domain (CBD). The DNA coding for this putative CBD was subcloned into pET-8c, an Escherichia coli expression vector. The protein produced under the direction of the recombinant plasmid, pET-CBD, had a high affinit...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34432-0