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pH‐induced transition and Zn 2+ ‐binding properties of bovine prolactin 1
Author(s) -
Permyakov Eugene A.,
Veprintsev Dmitry B.,
Deikus Gintaras Y.,
Permyakov Serge E.,
Kalinichenko Lina P.,
Grishchenko Valery M.,
Brooks Charles L.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00203-2
Subject(s) - chemistry , crystallography , radiochemistry
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 2×10 5 M −1 at pH 6.5 and 1×10 4 M −1 at pH 8.5. The pH dependence of both thermal stability and zinc binding surrounding the p K a of histidine suggests that these residues plays a key role in the structural integrity of bovine prolactin.