A Mutation Causing Reduced Biological Activity and Stability of Thyroxine-Binding Globulin Probably as a Result of Abnormal Glycosylation of the Molecule (original) (raw)
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1Department of Medicine, The University of Chicago Chicago, Illinois 60637; Department of Pediatrics, The University of Chicago Chicago, Illinois 60637; Department of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, The University of Chicago Chicago, Illinois 60637
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1Department of Medicine, The University of Chicago Chicago, Illinois 60637; Department of Pediatrics, The University of Chicago Chicago, Illinois 60637; Department of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, The University of Chicago Chicago, Illinois 60637
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1Department of Medicine, The University of Chicago Chicago, Illinois 60637; Department of Pediatrics, The University of Chicago Chicago, Illinois 60637; Department of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, The University of Chicago Chicago, Illinois 60637
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1Department of Medicine, The University of Chicago Chicago, Illinois 60637; Department of Pediatrics, The University of Chicago Chicago, Illinois 60637; Department of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, The University of Chicago Chicago, Illinois 60637
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1Department of Medicine, The University of Chicago Chicago, Illinois 60637; Department of Pediatrics, The University of Chicago Chicago, Illinois 60637; Department of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, The University of Chicago Chicago, Illinois 60637
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1Department of Medicine, The University of Chicago Chicago, Illinois 60637; Department of Pediatrics, The University of Chicago Chicago, Illinois 60637; Department of Biochemistry and Molecular Biology and Howard Hughes Medical Institute, The University of Chicago Chicago, Illinois 60637
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Received:
30 September 1988
Revision received:
07 December 1988
Accepted:
09 December 1988
Cite
Yuichi Mori, Susumu Seino, Kyoko Takeda, Irwin L. Flink, Yoshiharu Murata, Graeme I. Bell, Samuel Refetoff, A Mutation Causing Reduced Biological Activity and Stability of Thyroxine-Binding Globulin Probably as a Result of Abnormal Glycosylation of the Molecule, Molecular Endocrinology, Volume 3, Issue 3, 1 March 1989, Pages 575–579, https://doi.org/10.1210/mend-3-3-575
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Abstract
T4-binding globulin (TBG), a 54-kilodalton glycoprotein, is the major thyroid hormone transport protein in man. The exact nature of the mutations causing X chromosome-linked TBG deficiency, which affect about 1 in 2,500 newborn males, is unknown. Here we report the sequence of a unique variant TBG (TBG-Gary) encoding a protein with severely impaired T4 binding as well as decreased stability at 37 C, resulting in its rapid in vivo denaturation. A single nucleotide substitution in the codon for residue 96 of the mature protein replaces isoleucine with asparagine; this replacement creates an additional site for N-linked glycosylation. The anodal shift of TBG-Gary on isoelectric focusing gel electrophoresis suggests that this new site is likely glycosylated. Since glycosylation is required for TBG to assume its correct tertiary structure, but is not subsequently necessary for maintenance of the biological properties or stability of the molecule, we believe that the likely presence of additional carbohydrate probably affects a higher order structure of the molecule and is thus responsible for the reduced stability and hormone binding activity of TBG-Gary (TBGASN-96)
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Copyright © 1989 by The Endocrine Society
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