pH‐induced transition and Zn2+‐binding properties of bovine prolactin

FEBS Letters

Deikus, Gintaras Y.²  Brooks, Charles L.¹  Veprintsev, Dmitry B.²  Kalinichenko, Lina P.³  Permyakov, Eugene A.²  Permyakov, Serge E.²  Grishchenko, Valery M.³ 

[1] Department of Veterinary Biosciences and Ohio State Biochemistry Program, The Ohio State University, 1925 Coffey Rd., Columbus, OH 43210, USA;Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow region 142292, Russian Federation;Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow region 142292, Russian Federation

关键词: Prolactin;    Zinc binding;    Intrinsic fluorescence;    pH-induced transition;   

DOI  :  10.1016/S0014-5793(97)00203-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A pH-induced conformational transition was found in bovine prolactin within the physiologically significant pH region from 6.5 to 8.5. The thermal stability of prolactin at pH 6.5 is essentially higher than at pH 8.5. Bovine prolactin binds zinc ions with an apparent association constant of 2×10⁵ M⁻¹ at pH 6.5 and 1×10⁴ M⁻¹ at pH 8.5. The pH dependence of both thermal stability and zinc binding surrounding the pK _a of histidine suggests that these residues plays a key role in the structural integrity of bovine prolactin.

【 授权许可】

Unknown