Protective effect of small amounts of sodium dodecyl sulfate on the helical structure of bovine serum albumin in thermal denaturation

• Published in: Journal of colloid and interface science Vol. 257; no. 1; pp. 41 - 46
• Main Authors: Moriyama, Yoshiko, Kawasaka, Yoshie, Takeda, Kunio
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 2003; Elsevier
• Subjects: Amphiphilic material; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Bovine serum albumin; Cattle; Chemistry; Circular Dichroism; Cross-linking function; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; General and physical chemistry; General aspects, investigation methods; Hot Temperature; Protective effect on protein structure; Protein Denaturation - drug effects; Protein Renaturation - drug effects; Protein structure; Protein Structure, Secondary; Proteins; Secondary structure; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Sodium dodecyl sulfate; Sodium Dodecyl Sulfate - metabolism; Sodium Dodecyl Sulfate - pharmacology; Sulfuric Acid Esters; Surface physical chemistry; Surface-Active Agents - metabolism; Surface-Active Agents - pharmacology; Surface-active agents: properties; Surfactant; Thermal denaturation; Sodium dodecyl sulfate; Bovine serum albumin; Amphiphilic material; Cross-linking function; Thermal denaturation; Secondary structure; Protective effect on protein structure; Surfactant; Protein structure; Circular dichroism; Molecular structure; Preservation agent; Sodium compound; Serum albumin; Experimental study; Protein; Lauryl sulfate; Anionic surfactant; Concentration effect; Helical structure; Bovine serum albuins Thermal denaturation

In the presence of sodium dodecyl sulfate (SDS), the secondary structure of bovine serum albumin (BSA) was almost protected against thermal denaturation above 50 °C, where the structural change became irreversible. Beyond 30 °C, the helicity (66%) of the protein sharply decreased with rise of temper...