๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Characterization of denatured proteins by hydrophobic interaction chromatography: A preliminary study

โœ Scribed by Emilia Bramanti; Fabrizio Ferri; Chandra Sortino; Massimo Onor; Giorgio Raspi; Marcella Venturini


Publisher
Wiley (John Wiley & Sons)
Year
2003
Tongue
English
Weight
141 KB
Volume
69
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Purification of human plasma retinol-bin
โœ Rodolfo Berni; Simone Ottonello; Hugo L. Monaco ๐Ÿ“‚ Article ๐Ÿ“… 1985 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 332 KB

Human plasma retinol-binding protein has been purified to homogeneity by a simple method that requires an ammonium sulfate fractionation, a hydrophobic interaction chromatography on phenyl-Sepharose, which dissociates the complex between retinol-binding protein and its carrier, transthyretin, and a

Purification of some soybean proteins by
โœ Senyuk, V. I. ;Yattara, H. B. ;Vaintraub, I. A. ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 224 KB

Soybean glycinin and KUNITZ trypsin inhibitor were purified by hydrophobic chromatography on Phenyl Sepharose which removes the admixtures of more hydrophobic proteins and of some non-protein UV-absorbing substances. ## Zusammenfassung Reinigung einiger Sojabohnenproteine durch hydrophobe Chromat

Characterization of multimodal hydrophob
โœ Kristian Becker; Elisabeth Hallgren; Enrique Carredano; Ronnie Palmgren; Leif Bรผ ๐Ÿ“‚ Article ๐Ÿ“… 2009 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 309 KB

## Abstract Hydrophobic interaction chromatography (HIC) has been developed as a powerful technique for separating and purifying proteins. In this study, we have characterized the ability of new multimodal pHโ€HIC media to resolve proteins with only small differences in their primary structures. Thi

Optimization of hydrophobic interaction
โœ Marรญa Elena Lienqueo; Carolina Shene; Juan Asenjo ๐Ÿ“‚ Article ๐Ÿ“… 2009 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 423 KB

## Abstract This paper describes a methodology for optimizing performance of hydrophobic interaction chromatography (HIC) for protein mixtures in which Rate Model simulations and evaluation of cost function are used. The system under study was HIC of a twoโ€protein mixture (ฮฑโ€chymotrypsin and ฮฑโ€amyl

Identification and Characterization of H
โœ Sonja Hess; Frederick J. Cassels; Lewis K. Pannell ๐Ÿ“‚ Article ๐Ÿ“… 2002 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 85 KB

Virulence of enterotoxicogenic Escherichia coli is mediated by rodlike, rigid, highly hydrophobic proteins designated fimbriae or colonization factors (CFs). More than 20 different colonization factors have been described so far using predominantly immunological and genetic methods. To characterize