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Volumn 1121, Issue 2, 2006, Pages 209-218

Loading, stationary phase, and salt effects during hydrophobic interaction chromatography: α-Lactalbumin is stabilized at high loadings

(3) Fogle, Jace L a O'Connell, John P a Fernandez, Erik J a

a University of Virginia (United States)

Author keywords

Lactalbumin; Amide hydrogen deuterium exchange; Hydrophobic interaction chromatography; Protein loading; Stability

Indexed keywords

DEUTERIUM; PROTEINS; RESINS; SALTS; SATURATION (MATERIALS COMPOSITION); STABILITY;

Α-LACTALBUMIN; AMIDE HYDROGEN-DEUTERIUM EXCHANGE; HYDROPHOBIC INTERACTION CHROMATOGRAPHY (HIC); PROTEIN LOADING;

HYDROPHOBIC CHROMATOGRAPHY;

ALPHA LACTALBUMIN; AMIDE; SODIUM CHLORIDE;

ADSORPTION; ARTICLE; CHROMATOGRAPHY; DEUTERIUM HYDROGEN EXCHANGE; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN STABILITY;

ADSORPTION; CHROMATOGRAPHY, LIQUID; LACTALBUMIN; SALTS; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 33745266718 PISSN: 00219673 EISSN: None Source Type: Journal
DOI: 10.1016/j.chroma.2006.04.015 Document Type: Article

Times cited : (40)

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