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Volumn 277, Issue 2, 2004, Pages 285-291
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Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturation binding: The ionic strength effect
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Author keywords
Aggregation number; Albumin serum albumin; BSA; Protein surfactant interaction; Small angle X ray scattering; Sodium dodecyl sulfate; Surface tension
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Indexed keywords
AGGREGATES;
CHEMICAL BONDS;
IONIC STRENGTH;
MICELLES;
PROTEINS;
SODIUM COMPOUNDS;
BOVINE SERUM ALBUMIN (BSA);
SMALL ANGLE X RAY SCATTERING (SAXS);
BODY FLUIDS;
BOVINE SERUM ALBUMIN;
DODECYL SULFATE SODIUM;
SODIUM CHLORIDE;
ADDITION REACTION;
AQUEOUS SOLUTION;
ARTICLE;
BINDING AFFINITY;
CONCENTRATION RESPONSE;
FLUORESCENCE ANALYSIS;
IONIC STRENGTH;
MICELLE;
MOLECULAR DYNAMICS;
MOLECULAR INTERACTION;
MOLECULAR MECHANICS;
MOLECULAR MODEL;
OXYGEN SATURATION;
PARTICLE SIZE;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DEGRADATION;
RADIATION SCATTERING;
RANDOMIZATION;
REACTION ANALYSIS;
SEGREGATION DISTORTION;
SURFACE TENSION;
ANIMALS;
CATTLE;
FLUORESCENCE;
MICELLES;
OSMOLAR CONCENTRATION;
PARTICLE SIZE;
SERUM ALBUMIN, BOVINE;
SODIUM DODECYL SULFATE;
SURFACE PROPERTIES;
X-RAY DIFFRACTION;
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EID: 4043159165
PISSN: 00219797
EISSN: None
Source Type: Journal
DOI: 10.1016/j.jcis.2004.04.059 Document Type: Article |
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Times cited : (53)
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References (32)
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