OCP2 is one of the most abundant proteins in the organ of Corti (OC), compr
ising approximately 5% of the total protein in the supporting cell populati
on. Although the very close homolog, Skp1p, has been implicated in regulati
ng cell-cycle progression, the function of OCP2 in the terminally different
iated cochlea is presently unknown. We have purified recombinant OCP2 from
Escherichia coli and examined the protein by analytical ultracentrifugation
. Interestingly, sedimentation equilibrium data collected at 20 degrees C u
nequivocally indicate that, at the concentrations present in the OC, free O
CP2 would exist as a dimeric species. The apparent sedimentation coefficien
t is independent of concentration at loading concentrations between 10 and
100 mu M, indicating the absence of a significant monomer-dimer equilibrium
in this concentration range. The functional significance of this Finding i
s discussed. (C) 1998 Elsevier Science B.V. All rights reserved.