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langmuir aggregation of alkali blue 6b in proteins: Study and application
Author(s) -
Gao HongWen,
Mei HouDong
Publication year - 2002
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/1616-5195(200208)2:6<280::aid-mabi280>3.0.co;2-z
Subject(s) - chemistry , ovalbumin , myoglobin , bovine serum albumin , adsorption , langmuir , protein adsorption , langmuir adsorption model , chromatography , organic chemistry , immune system , immunology , biology
Abstract The formation of microelectrostatic fields in biopolymers causes the adsorption of stain molecules in protein. The interactions between the dye alkali blue 6B (AB6B) and four proteins, bovine serum albumin (BSA), human γ ‐globulin ( γ ‐G), horse myoglobin (Mb) and ovalbumin (OVA), were studied by the microphase adsorption/spectral correction technique. It was observed that the interactions obey the Langmuir isothermal adsorption. The Langmuir equilibrium constants of all the aggregates were determined. Interestingly, the adsorption of AB6B has no relation to the array sequence of amino acid residues, and an electrostatic field consists of constant amino acid residues. The novel method has been applied satisfactorily to the determination of the total protein content in two different samples.