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

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

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


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 x 105 M-1 at pH 6.5 and 1 x 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.

Original languageEnglish
Pages (from-to)273-276
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - 1 Apr 1997
Externally publishedYes


  • Intrinsic fluorescence
  • Prolactin
  • Zinc binding
  • pH-induced transition


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