The denaturing action of lysophosphatidylcholine as studied by calorimetric and rheological techniques

✍ Scribed by B. Egelandsdal; K. Fretheim; O. Harbitz

• Book ID: 103041653
• Publisher: Elsevier Science
• Year: 1991
• Tongue: English
• Weight: 411 KB
• Volume: 57
• Category: Article
• ISSN: 0009-3084
• DOI: 10.1016/0009-3084(91)90052-d

✦ Synopsis

The potency of lysophosphatidylcholine to perturb protein structure was investigated by differential scanning calorimetry and theological measurements using myosin as a model protein. At physiological ionic strength (0.15 M NaCI) 5 mM lysophosphatidylcholine produced a detectable reduction in the protein's enthalphy of denaturation, while concentrations < 2 mM had no effect. At higher salt concentrations (0.6 M NaCI) lower concentrations of lysophosphatidylcholine were needed in order to reduce the enthalphy of denaturation. Also, the changes in myosin conformation, as judged from calorimetric measurements, became more extensive as the incubation temperature for myosin-lysophosphatidyicholine systems was increased from 10 ° to 30°C. Rheoiogical techniques allowed detection of changes in the structure of filaments of myosin (in 0.15 M) upon addition of 0.2 mM lysophosphatidylcholine. The denaturing action of lysophosphatidylcholine is compared to the more familiar detergent sodium dodecyl sulphate.