منابع مشابه
Sodium dodecyl sulphate electrophoresis of wheat gliadins.
Polypeptide chain weights of a-, 8and y-gliadin fractions have been estimated by polyacrylamide gel electrophoresis in the presence of mercaptoethanol and sodium dodecyl sulphate. Values lie in the range 32 000 to 44 OOO. When available data on the amino acid analyses were adjusted and compared, significant similarities emerged. It is suggested that these gliadins contain a minimum of 4 cystine...
متن کاملMobility of sodium dodecyl sulphate - protein complexes.
Reduced and unreduced lysozyme aggregates formed by formaldehyde cross-linking comprise a set of model compounds for studying the effects of protein conformation on the electrophoretic mobilities of sodium dodecyl sulphate-protein complexes. The reduced aggregates were indistinguisable from normal proteins, but the unreduced aggregates migrated anomalously fast by about 14%. Contrary to expecta...
متن کاملThermal Analysis of Adenosine Deaminase in the Presence of Sodium N-Dodecyl Sulphate
The thermal denaturation of adenosine deaminase (ADA) has been investigated in the presence of sodium n-dodecyl sulphate (SDS) over the temperature range of (293-363K) in 2.5 mM phosphate buffer, pH 6.4 by temperature scanning spectroscopy. The interaction of SDS caused the folding of adenosine deaminanse resulting in a decrease of TH (temperature of minimum solubility), TS<...
متن کاملCOMPARATIVE STRUCTURAL STABILITY OF HISTONES BY INTERACTION OF SODIUM NDODECYL SULPHATE
The interaction of sodium n-dodecyl sulphate (SDS) with histones in phosphate buffer pH 6.4 has been studied spectroscopically and by equilibrium dialysis. The enthalpies of interaction and the spectroscopic data suggest different structural stability for histones-SDS interaction. The linear relation between enthaly and absorbtion was determined by the equation of m= , where m is the sta...
متن کاملTHERMODYNAMIC STUDIES OF THE INTERACTION OF SODIUM N-DODECYL, SULPHATE WITH CALF - THYMUS WISTONE H3
The binding of Sodium n-dodecyl sulphate (SDS) to histone H3 was studied in the pH range 3.2-10 by equilibrium dialysis at 27? and 3 7 ?c .T he binding data have been used to obtain the Gibbs free energy of interaction using a theoretical model of the Wyman binding potential; and the enthalpy of interaction from the temperature dependence of theequilibriumconstantsfronr theVan't Hoff re1ati...
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ژورنال
عنوان ژورنال: J. Chem. Soc., Trans.
سال: 1884
ISSN: 0368-1645
DOI: 10.1039/ct8844500686