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The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol–Sepharose

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Purification of a cystic fibrosis plasmid vector for gene therapy using hydrophobic interaction chromatography

inferredcites →https://doi.org/10.1002/9780470027318openalex-snapshot

Encyclopedia of Analytical Chemistry

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Protein unfolding during reversed‐phase chromatography: II. Role of salt type and ionic strength

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Adsorption of Bovine Serum Albumin and Lysozyme on Hydrophobic Calcium Hydroxyapatites

inferredcites →https://doi.org/10.1016/0001-8686(86)80012-4openalex-snapshot

Adsorption of proteins from solution at the solid-liquid interface

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Fundamentals of preparative and nonlinear chromatography

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Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series

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Thermodynamic analysis of the effect of concentrated salts on protein interaction with hydrophobic and polysaccharide columns

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Thermal behavior of proteins in high-performance hydrophobic-interaction chromatography On-line spectroscopic and chromatographic characterization

inferredcites →https://doi.org/10.1016/0021-9673(95)01163-3openalex-snapshot

Hydrophobic interaction chromatography of Chromobacterium viscosum lipase on polyethylene glycol immobilized on Sepharose

inferredcites →https://doi.org/10.1016/0166-0934(81)90072-0openalex-snapshot

Removal of hepatitis B virus from a concentrate of coagulation factors II, VII, IX and X by hydrophobic interaction chromatography

inferredcites →https://doi.org/10.1016/0378-4347(94)00550-oopenalex-snapshot

Influence of salts on protein interactions at interfaces of amphiphilic polymers and adsorbents

inferredcites →https://doi.org/10.1016/j.chroma.2003.07.010openalex-snapshot

Effect of salts and temperature on the adsorption of bovine serum albumin on polypropylene glycol-Sepharose under linear and overloaded chromatographic conditions

inferredcites →https://doi.org/10.1016/s0021-9673(00)01034-7openalex-snapshot

Flow microcalorimetric measurements for bovine serum albumin on reversed-phase and anion-exchange supports under overloaded conditions

inferredcites →https://doi.org/10.1016/s0021-9673(01)01340-1openalex-snapshot

Characterization of enthalpic events in overloaded ion-exchange chromatography

inferredcites →https://doi.org/10.1016/s0021-9673(01)84176-5openalex-snapshot

Study of the retention mechanism of proteins in hydrophobic interaction chromatography

inferredcites →https://doi.org/10.1016/s0021-9673(01)91648-6openalex-snapshot

Salt-mediated retention of proteins in hydrophobic-interaction chromatography

inferredcites →https://doi.org/10.1016/s0021-9673(01)94777-6openalex-snapshot

Preparation of adsorbents for biospecific affinity chromatography

inferredcites →https://doi.org/10.1016/s0021-9673(96)00978-8openalex-snapshot

Protein retention in hydrophobic interaction chromatography: modeling variation with buffer ionic strength and column hydrophobicity

inferredcites →https://doi.org/10.1016/s0021-9673(99)00619-6openalex-snapshot

Hydrophobic interaction chromatography of Chromobacterium viscosum lipase on polypropylene glycol immobilised on Sepharose

inferredcites →https://doi.org/10.1016/s0021-9673(99)01118-8openalex-snapshot

Study of hydrophobic interaction adsorption of bovine serum albumin under overloaded conditions using flow microcalorimetry

inferredcites →https://doi.org/10.1016/s0021-9673(99)01231-5openalex-snapshot

Microcalorimetric studies of interactions between proteins and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density and the amount of bound protein

inferredcites →https://doi.org/10.1016/s0076-6879(00)x0224-8openalex-snapshot

Guide to Protein Purification

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Hydrophobic interaction chromatography of proteins

inferredcites →https://doi.org/10.1021/ac00109a038openalex-snapshot

Influence of the Chain Length and Surface Density on the Conformation and Mobility of n-Alkyl Ligands Chemically Immobilized onto a Silica Surface

inferredcites →https://doi.org/10.1021/ac9600868openalex-snapshot

Response to Comment on “Influence of the Chain Length and Surface Density on the Conformation and Mobility of n-Alkyl Ligands Chemically Immobilized onto a Silica Surface”

inferredcites →https://doi.org/10.1021/ie9507437openalex-snapshot

Retention Thermodynamics in Hydrophobic Interaction Chromatography

inferredcites →https://doi.org/10.1073/pnas.93.6.2290openalex-snapshot

Temperature effects in hydrophobic interaction chromatography.

inferredcites →https://doi.org/10.1081/ss-120002734openalex-snapshot

Studies on hydrophobic interaction adsorption of bovine serum albumin on polypropylene glycol–sepharose under overloaded conditions

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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