Native disulfide bonds in plasma retinol-binding protein are not essential for all-trans-retinol-binding activity.

Abstract excerpt

A human plasma retinol-binding protein (RBP) mutant, named RBP-S, has been designed and produced in which the six native cysteine residues, involved in the formation of three disulfide bonds, have been replaced with serine. A hexa-histidine tag was also added to the C-terminus of RBP for ease of purification. The removal of the disulfide bonds led to a decrease in the affinity of RBP for all trans-retinol. Data...

Topics

• Circular Dichroism
• Cloning, Molecular
• Disulfides
• Kinetics
• Ligands
• Mutation
• Protein Binding
• Retinol-Binding Proteins
• Retinol-Binding Proteins, Plasma
• Thermodynamics
• Vitamin A