Hapak R C, Zhao H, Henzl M T
Biochemistry Department, University of Missouri, Columbia 65211.
FEBS Lett. 1994 Aug 1;349(2):295-300. doi: 10.1016/0014-5793(94)00691-1.
CPV3, the third parvalbumin isoform to be identified in the chicken, is produced exclusively in the thymus gland. Although parvalbumins are typically cysteine-deficient, CPV3 contains two cysteine residues, at positions 18 and 72. The reported three-dimensional parvalbumin structures suggest that the side chain of cysteine-72 should be solvent-accessible. Accordingly, we find that CPV3 readily forms disulfide-linked oligomers in the absence of reducing agents. The reaction, employing either O2 or ferricyanide ion as the oxidant, is apparently restricted to the Ca(2+)-bound form of the protein. The differing reactivity of the Ca2+, Mg2+, and apo-forms has significant structural implications.
