Premium
Involvement of lysine residues in the binding of hGH and bGH to somatotropic receptors
Author(s) -
Martal J.,
Chêne N.,
de la Llosa P.
Publication year - 1985
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 - 10.1016/0014-5793(85)81089-9
Subject(s) - lysine , somatotropic cell , receptor , chemistry , biochemistry , growth hormone , hormone , amino acid
The biological activities of human (hGH) and bovine (bGH) growth hormone derivatives obtained by chemical modification of the lysine residues were studied by radioreceptor assays using rabbit liver homogenates for somatotropic activity (SA). Control treatment with BH 4 − had a very slight effect on the SA, whereas the methylation and ethylation drastically reduced the acitivty of both hormones. Guanidination of these hormones and even acetimidination at a lower rate are accompanied by a considerable loss of biological activity. These results show the involvement of lysine residues in the interaction of hGH and bGH with somatotropic receptors. The structure‐function relationship of these molecules is discussed, suggesting that the lysine or arginine residues in positions 41, 64, 70 and 115 might be particularly implicated.