Importance of arginine residues in the determination of the biological activity of human corticosteroid-binding globulin
La capacité de la transcortine humaine de lier les corticostéroïdes est dépendante du pH et gouvernée en milieu alcalin par le pK des résidus d'arginine. Il n'y a pas d'arginine essentielle dans le site de liaison. La perte de l'activité biologique est rapide et complète dès qu...
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Published in | Biochimie Vol. 65; no. 10; pp. 579 - 583 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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Paris
Elsevier Masson SAS
01.10.1983
Elsevier |
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Abstract | La capacité de la transcortine humaine de lier les corticostéroïdes est dépendante du pH et gouvernée en milieu alcalin par le pK des résidus d'arginine. Il n'y a pas d'arginine essentielle dans le site de liaison. La perte de l'activité biologique est rapide et complète dès qu'un résidu d'arginine est modifié par le phénylglyoxal. Il y a également une transconformation de la molécule de transcortine. C'est pourquoi l'étonnante stabilité de la transcortine à pH 11,5 peut être expliquée par une grande dépendance de la structure tertiaire vis-à-vis de l'intégrité d'un résidu d'arginine: aussi longtemps que l'état d'ionisation de celui-ci n'est pas changé (pH < pK du groupement guanidyl), la structure tertiaire de la transcortine biologiquement active est conservée en milieu alcalin.
The binding activity of human corticosteroid-binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential arginine residue is located in the binding site. The loss of biological activity is rapid and complete as soon as one arginine residue is modified by phenylglyoxal. There is also a transconformation of the CBG molecule. Therefore the surprising stability of CBG up to pH 11.5 may be explained by a large dependence of the CBG tertiary structure on the integrity of one arginine residue: as long as the ionized state of this single residue is not changed (pH < pK of the guanidyl group) the tertiary structure of the biologically active CBG is maintained in alkaline pH ranges. |
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AbstractList | The binding activity of human corticosteroid-binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential arginine residues is located in the binding site. The loss of biological activity is rapid and complete as soon as one arginine residue is modified by phenylglyoxal. There is also a transconformation of the CBG molecule. Therefore the surprising stability of CBG up to pH 11.5 may be explained by a large dependence of the CBG tertiary structure on the integrity of one arginine residue : as long as the ionized state of this single residue is not changed (pH less than pK of the guanidyl group) the tertiary structure of the biologically active CBG is maintained in alkaline pH ranges. La capacité de la transcortine humaine de lier les corticostéroïdes est dépendante du pH et gouvernée en milieu alcalin par le pK des résidus d'arginine. Il n'y a pas d'arginine essentielle dans le site de liaison. La perte de l'activité biologique est rapide et complète dès qu'un résidu d'arginine est modifié par le phénylglyoxal. Il y a également une transconformation de la molécule de transcortine. C'est pourquoi l'étonnante stabilité de la transcortine à pH 11,5 peut être expliquée par une grande dépendance de la structure tertiaire vis-à-vis de l'intégrité d'un résidu d'arginine: aussi longtemps que l'état d'ionisation de celui-ci n'est pas changé (pH < pK du groupement guanidyl), la structure tertiaire de la transcortine biologiquement active est conservée en milieu alcalin. The binding activity of human corticosteroid-binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential arginine residue is located in the binding site. The loss of biological activity is rapid and complete as soon as one arginine residue is modified by phenylglyoxal. There is also a transconformation of the CBG molecule. Therefore the surprising stability of CBG up to pH 11.5 may be explained by a large dependence of the CBG tertiary structure on the integrity of one arginine residue: as long as the ionized state of this single residue is not changed (pH < pK of the guanidyl group) the tertiary structure of the biologically active CBG is maintained in alkaline pH ranges. The binding activity of human corticosteroid binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential arginine residue is located in the binding site. The loss of biological activity is rapid and complete as soon as one arginine residue is modified by phenylglyoxal. There is also a transconformation of the CBG molecule. Therefore the surprising stability of CBG up to pH 11.5 may be explained by a large dependence of the CBG tertiary structure on the integrity of one arginine residue: as long as the ionized state of this single residue is not changed (pH < pK of the guanidyl group) the tertiary structure of the biologically active CBG is maintained in alkaline pH ranges. |
Author | Dautrevaux, M. Perini, J.M. Le Gaillard, F. Aubert, J.P. |
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Keywords | site de liaison transcortin transcortine phenylglyoxal corticosteroid-binding globulin binding site Human Corticosteroid Binding protein Chemical modification Steroid hormone Transcortin Molecular interaction Binding site |
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References | Le Gaillard, Racadot, Racadot-Leroy, Dautrevaux (bib1) 1974; 56 Takahashi (bib6) 1977; 81 Takahashi (bib7) 1977; 81 Mickelson, Forsthoefel, Westphal (bib10) 1981; 20 Le Gaillard, Racadot, Aubert, Dautrevaux (bib9) 1982; 57 Le Gaillard, Dautrevaux (bib4) 1977; 495 Stroupe, Harding, Forsthoefel, Westphal (bib3) 1978; 17 Le Gaillard, F. (Unpublished result). Takahashi (bib8) 1962; 52 Le Gaillard, Han, Dautrevaux (bib2) 1975; 57 Le Gaillard (10.1016/S0300-9084(83)80108-4_bib2) 1975; 57 Takahashi (10.1016/S0300-9084(83)80108-4_bib6) 1977; 81 10.1016/S0300-9084(83)80108-4_bib5 Takahashi (10.1016/S0300-9084(83)80108-4_bib7) 1977; 81 Le Gaillard (10.1016/S0300-9084(83)80108-4_bib9) 1982; 57 Mickelson (10.1016/S0300-9084(83)80108-4_bib10) 1981; 20 Takahashi (10.1016/S0300-9084(83)80108-4_bib8) 1962; 52 Stroupe (10.1016/S0300-9084(83)80108-4_bib3) 1978; 17 Le Gaillard (10.1016/S0300-9084(83)80108-4_bib1) 1974; 56 Le Gaillard (10.1016/S0300-9084(83)80108-4_bib4) 1977; 495 |
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Snippet | La capacité de la transcortine humaine de lier les corticostéroïdes est dépendante du pH et gouvernée en milieu alcalin par le pK des résidus d'arginine. Il... The binding activity of human corticosteroid-binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential... The binding activity of human corticosteroid binding globulin (CBG) is pH dependent and governed in alkaline pH ranges by the pK of arginine. No essential... |
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SubjectTerms | Analytical, structural and metabolic biochemistry Arginine Binding and carrier proteins binding site Biological and medical sciences Circular Dichroism corticosteroid-binding globulin Fundamental and applied biological sciences. Psychology Humans Hydrocortisone - metabolism Hydrogen-Ion Concentration Kinetics phenylglyoxal Phenylglyoxal - metabolism Protein Binding Protein Conformation Proteins site de liaison transcortin Transcortin - metabolism transcortine |
Title | Importance of arginine residues in the determination of the biological activity of human corticosteroid-binding globulin |
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