FEBS Letters | |
1H‐NMR studies of the histidine residues of human choriogonadotropin and its α‐ and β‐subunits | |
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
【 预 览 】
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RO201912020283896ZK.pdf | 378KB | download |