May 1, 1976

Studies of human transcortin at different pHs: circular dichroism, polymerisation and binding affinity

FEBS Letters
F Le GaillardM H Loucheux-Lefebvre


The transcortin we have used in this work is extremely pure. This was shown by the polymerisation observed at pH 4. This polymerisation is never observed with an impure form of transcortin [4]. Moreover, since it is known that the presence of cortisol in the binding site is an essential condition to the activity of purified transcortin [5], it appears that a correlation between the secondary structure and the biological activity of the transcortin exists. The results we have obtained are summarized below: (1) The inhibition of the transcortin binding capacity essentially takes place between pH 5 and 4. (2) A reorganisation of the structure of the protein moiety is observed between pH 6.5 and 5.9. (3) A decrease of the helicity ratio is observed between pH 5 and 4. It appears therefore that, in the limits of experimental accuracy of CD measurements to determine the amount of beta-structure, no appreciable change of binding activity is taking place after the appearance of a large percentage of beta-structure between pH 6.5 and 6. On the other hand, the sudden decrease of protein activity at low pH is likely to be correlated with the disappearance of a well-defined helical region. Other biochemical and physical experiments would b...Continue Reading

Mentioned in this Paper

Structure-Activity Relationship
Ligand Binding Domain
Protein Conformation
Metabolic Inhibition
Circular Dichroism, Vibrational
Binding Activity [MoA]
Protein Activity

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