1H‐NMR studies of the histidine residues of human choriogonadotropin and its α‐ and β‐subunits

FEBS Letters

Roberts, G.C.K.²  Frankenne, F.¹  Birdsall, B.²  Maghuin-Rogister, G.³ 

[1] Laboratoire d'Endocrinologie Expérimentale et Clinique, Institut de Pathologie, Université de Liège, B23-Sart Tilman, B4000 Liège Belgium;Division of Molecular Pharmacology, National Institute for Medical Research, Mill Hill, London, NW7 1AA, England;Faculté de Médecine Vétérinaire (Cureghem), Université de Liège, 45 rue des Vétérinaires, B1070 Bruxelles, Belgium

关键词: Choriogonadotropin;    Nuclear Magnetic Resonance (NMR);    Histidine;    Subunit in teractions;    Glycoprotein hormones;   

DOI  :  10.1016/0014-5793(83)80068-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The pH-dependence of the chemical shifts of the imidazole C2-proton resonances of the 4 histidine residues of human choriogonadotropin has been determined in the intact hormone and in its isolated α- and β-subunits. The single histidine of the β-subunit and two of the histidines of the α-subunit show only minor changes in pK when the subunits recombine. However, one histidine of the α-subunit, tentatively identified as Hisα83, has a very low pK (≤2.4) in the isolated subunit and increases markedly on recombination with the β-subunit, strongly suggesting that a conformational change occurs. This behaviour is closely similar to that reported earlier for porcine lutropin.

【 授权许可】

Unknown