نتایج جستجو برای: polyacrylamide gels

تعداد نتایج: 31220  

Journal: :The Journal of Cell Biology 1971
Arthur R. Ugel

Histochemical and ultrastructural studies demonstrate that keratohyalin can be mobilized from fresh specimens of cattle hoof epidermis by 1.0 M potassium phosphate buffer (pH 7.0). Macroaggregates with histochemical characteristics identical to those of in situ keratohyalin granules (staining by Harris' hematoxylin, Congo red, diazotized sulfanilic acid, sodium alizarin sulfonate, toluidine blu...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1986
L Ulanovsky M Bodner E N Trifonov M Choder

Curved DNA molecules and unusually small circles have been obtained by ligation of synthetic 21-base precursors: (sequence in text). The ligation resulted in the formation of double-stranded oligo-(precursor)s possessing a strong 10.5-base-pair (bp) periodicity of the runs of adenines. Two-dimensional polyacrylamide gel electrophoresis of the ligation products showed two distinct families of sp...

Journal: :BioTechniques 1998
P D Rye N V Bovin

Immobilized neoglycoconjugates covalently cross-linked into a polyacrylamide gel can be used to detect and characterize carbohydrate-binding proteins. The neoglycoconjugates comprise two active groups, saccharide and allyl, located on a poly(2-hydroxyethylacrylamide) backbone. The allyl group cross-links with the polyacrylamide gel matrix, while the saccharide groups are available for specific ...

Journal: :BioTechniques 1998
J A Rodzen J J Agresti G Tranah B May

Laser scanners from Molecular Dynamics (Sunnyvale, CA, USA) or Hitachi Scientific Instruments (Mountain View, CA, USA) are being used increasingly to detect DNA in polyacrylamide gels. The standard technique for visualizing DNA is to separate the plates of a gel and pour a diluted nucleic acid stain such as ethidium bromide or SYBR Green I [from Molecular Probes (Eugene, OR, USA); also markete...

Journal: :The Biochemical journal 1980
R W Evans J Williams

The denaturation of transferrin by urea has been studied by (a) electrophoresis in polyacrylamide gels incorporating a urea gradient, (b) measurements of the loss of iron-binding capacity and (c) u.v. difference spectrometry. In human serum transferrin and hen ovotransferrin the N-terminal and C-terminal domains of the iron-free protein were found to denature at different urea concentrations.

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