Thyroxine-Protein Interactions
نویسندگان
چکیده
منابع مشابه
Thyroxine-protein interactions. Interaction of thyroxine and triiodothyronine with human thyroxine-binding globulin.
The effect of temperature on the binding of thyroxine and triiodothyronine to thyroxine-binding globulin has been studied by equilibrium dialysis. Inclusion of ovalbumin in the dialysis mixture stabilized thyroxine-binding globulin against losses in binding activity which had been found to occur during equilibrium dialysis. Ovalbumin by itself bound the thyroid hormones very weakly and its bind...
متن کاملThyroxine-thyroid hormone receptor interactions.
Thyroid hormone (TH) actions are mediated by nuclear receptors (TRs alpha and beta) that bind triiodothyronine (T(3), 3,5,3'-triiodo-l-thyronine) with high affinity, and its precursor thyroxine (T(4), 3,5,3',5'-tetraiodo-l-thyronine) with lower affinity. T(4) contains a bulky 5' iodine group absent from T(3). Because T(3) is buried in the core of the ligand binding domain (LBD), we have predict...
متن کاملDiscovering Domains Mediating Protein Interactions
Background: Protein-protein interactions do not provide any direct information regarding the domains within the proteins that mediate the interactions. The majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. Most of the former studies focus only on interacting domain pairs. However they do not consider the in...
متن کاملRelative rates of transcapillary movement of free thyroxine, protein-bound thyroxine, thyroxine-binding proteins, and albumin.
The rate of appearance of labeled thyroxine (T4) and albumin in lymph from various areas after simultaneous i.v. injection of the labeled substances in conscious ambulatory sheep has been used to estimate the relative rates of transcapillary movement of stable T4 and albumin. Labeled T4 appeared in hepatic lymph at the same rate as albumin. In intestinal and leg lymph, labeled T4 appeared eight...
متن کاملThyroxine-Protein Interactions I. BINDING OF THYROXI?;E TO HUnIAN SERUhI ALBUiVIIN AIVD ~IODII~IED ALBUiWIKS*
In previous reports (1, 2), it was suggested that the binding of thyroxine to human serum albumin resulted primarily from an electrostatic interaction between anionic portions of the thyroxine molecule and cationic sites on t.he protein. From the reduction in thyroxine binding exhibited by acetylated albumin preparations, it seemed likely that part of the reactive cationic sites were made up of...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93469-1