FEBS Letters | |
Oligomerization of an avian thymic parvalbumin Chemical evidence for a Ca2+‐specific conformation | |
Henzl, Michael T.1  Hapak, Raymond C.1  Zhao, Hongmei1  | |
[1] Biochemistry Department, 117 Schweitzer Hall, University of Missouri, Columbia, MO 65211, USA | |
关键词: Parvalbumin; Ca2+-binding protein; Disulfide bond; ATH; avian thymic hormone; CPV3; chicken parvalbumin isoform 3; EGTA; [ethylene-bis-(oxyethylenenitrilo)]tetraacetic acid; DTT; dithiothreitol; DTNB; 5; 5′-dithio-bis-(2-nitrobenzoate); HEPES; 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid; MES; 2-(N-morpholino)ethanesulfonic acid; PAGE; polyacrylamide gel electrophoresis; PCR; polymerase chain reaction; CD site; the metal ion-binding site in the parvalbumins flanked by the C and D helical segments; EF site; the metal ion-binding site in the parvalbumins flanked by the E and F helical segments; | |
DOI : 10.1016/0014-5793(94)00691-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 Ca2+-bound form of the protein. The differing reactivity of the Ca2+, Mg2+, and apo-forms has significant structural implications.
【 授权许可】
Unknown
【 预 览 】
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