http://www.cnr.it/ontology/cnr/individuo/prodotto/ID39158
Characterization of Denatured Proteins by Hydrophobic Interaction Chromatography: a preliminary study (Articolo in rivista)
- Type
- Label
- Characterization of Denatured Proteins by Hydrophobic Interaction Chromatography: a preliminary study (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Alternative label
Bramanti E., Ferri F., Sortino C., Onor M., Raspi G., Venturini M. (2003)
Characterization of Denatured Proteins by Hydrophobic Interaction Chromatography: a preliminary study
in Biopolymers (Print)
(literal)
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- Bramanti E., Ferri F., Sortino C., Onor M., Raspi G., Venturini M. (literal)
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- Pubblicazione su rivista internazionale (Impact Factor 2002=2.37) (literal)
- Note
- ISI Web of Science (WOS) (literal)
- Titolo
- Characterization of Denatured Proteins by Hydrophobic Interaction Chromatography: a preliminary study (literal)
- Abstract
- In this preliminary study hydrophobic interaction chromatography (HIC) is proposed as a good tool in order to detect conformational changes induced by chemical denaturants in two globular proteins, cytochrome C (Cyt C) and myoglobin (MYO). Alterations in protein structure were manifested chromatographically by reproducible changes in peak heights, retention time, and appearance of multiple peaks. The HIC behavior of the two model proteins denatured by guanidinium thyocyanate (GdmSCN) was investigated, keeping constant various concentrations of urea in the mobile phase in a TSK-Gel Phenyl-5PW column (TosoBiosep). Suitable elution conditions
provide evidence of the simultaneous presence of two denatured forms in the case of MYO, and sequential different denatured states of Cyt C. (literal)
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