Involvement of lysine residues in the binding of hGH and bGH to somatotropic receptors

FEBS Letters

Martal, J.¹  de la Llosa, P.²  Chêne, N.¹ 

[1]Laboratoire de Physiologie de la Lactation, INRA, 78350 Jouy-en-Josas, France

[2]Laboratoire des Hormones Polypeptidiques, CNRS, 91190 Gif-sur-Yvette, France

关键词: Human growth hormone;    Bovine growth hormone;    Human chorionic somatomammotropin;    Lysine residue;    Receptor;   

DOI  :  10.1016/0014-5793(85)81089-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 BH₄ ⁻ 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.

【 授权许可】

Unknown