Biochemical characterization of the minor immunophilins
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Updated: Oct 17, 2026
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
Published on: June 30, 2019
D L Davis1, J N Murthy, S J Soldin
1Department of Laboratory Medicine, Children's National Medical Center, Washington, DC 20010, USA.
Objective:
We present biochemical characterization of the previously described 14 kDa, 37 kDa, and 52 kDa immunophilins and a newly identified 5-8 kDa immunophilin.
Design And Methods:
Proteins were tested for the following enzymatic activities-rotamase, G3PDH, protein kinase C, cAMP dependent protein kinase-and for the ability to inhibit calcineurin phosphatase when complexed with tacrolimus (FK506).
Results:
The 5-8 kDa protein, like the other minor immunophilins, lacks rotamase activity. Since the 37 kDa possesses G3PDH activity, the 5-8 kDa protein, 14 kDa protein, and 52 kDa protein were all tested and found to lack G3PDH activity. Additional work shows that none of the minor immunophilins possess protein kinase C or cyclic AMP-dependent protein kinase activity and that the 37 kDa and 5-8 kDa and probably the 52 kDa proteins are capable of inhibiting calcineurin phosphatase when bound to tacrolimus.
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