Results 131 to 140 of about 13,578 (179)

Interaction of carbohydrate and protein in thyroxine binding globulin

Biochemistry, 1985
The fluorescence properties of human thyroxine binding globulin were evaluated during enzymatic deglycosylation by using both neuraminidase and a mixture of glycosidases. Three fluorescent chromophores, one intrinsic and two extrinsic, were monitored, and all showed changes in fluorescent parameters that have been interpreted in terms of a loss of ...
S, Grimaldi, J, Robbins, H, Edelhoch
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Thermal Stability of Serum Thyroxine-Binding Proteins

The Journal of Clinical Endocrinology & Metabolism, 1971
ABSTRACT The thyroxine-binding capacity of normal human blood serum after heating to 60 C was determined by paper electrophoresis. The denaturation of TBG by heat resulted in decrease of its binding capacity. The process of denaturation is strictly a reaction of the first order.
Y, Takemura, G, Hocman, K, Sterling
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A cellular thyroxine-binding protein fraction

Biochimica et Biophysica Acta, 1958
Abstract Evidence is presented of the existence of a protein fraction in rat skeletal muscle that is capable of binding l -thyroxine and 3:5:3′-triiodo- l -thyronine in physiological concentrations. As revealed by electrophoretic analysis, the specific protein fraction has a mobility intermediate between those of fractions “l” and “m” of globular ...
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Cytosolic thyroxine-binding protein and brain development

Molecular and Cellular Endocrinology, 1980
The properties of cytosolic thyroxine binding protein were studied in the cortex and cerebellum of the rat at different stages of postnatal development: (1) Polyacrylamide-gel electrophoretic analysis showed that rat-brain cortex and cerebellum contain the same cytosolic thyroxine-binding protein which is very similar to the liver-corresponding entity.
A M, Lennon, J, Osty, J, Nunez
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Thyroxine-binding Protein in the Serum of Rabbit Fœtuses

Nature, 1958
HUMAN serum contains a thyroxine-binding protein which moves to a position between the α1 and α2 globulins on paper electrophoresis in a barbiturate buffer1. We have investigated the thyroxine-binding power of maternal and fœtal serum taken from pregnant rabbits at different stages of pregnancy.
C, OSORIO, N B, MYANT
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Detection of a Thyroxine-Binding Protein Physicochemically Similar to Serum Thyroxine-Binding Globulin in Normal Human Urine

The Journal of Clinical Endocrinology & Metabolism, 1979
Urine samples from 10 normal adult males were analyzed for T4-binding globulin (TBG) employing a sensitive and specific RIA for serum TBG. Urine TBG was detected at a concentration of 1.74 +/- 0.87 microgram/100 ml (mean +/- SD). The excretion rate was 13.2 +/- 6.5 microgram/g creatinine. There was no correlation between the daily excretion rate of TBG
L A, Gavin, F A, McMahon, J N, Castle, R R, Cavalieri   +3 more
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Relation of plasma thyroxine binding to thyroidal activity and determination of thyroxine binding proteins in a turtle, Pseudemys scripta

General and Comparative Endocrinology, 1990
The ability of plasma to bind thyroxine (T4) was examined in the turtle, Pseudemys scripta, in relation to variations in thyroidal state associated with age, sex, environment, and surgical and chemical manipulations. Relative plasma binding activity was assessed by use of binding to [125I]T4 on minicolumns of Sephadex G-25 (fine).
P, Licht, R J, Denver, D L, Stamper
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HYPERTHYROIDISM AND DECREASED THYROXINE BINDING BY SERUM PROTEINS*

The Journal of Clinical Endocrinology & Metabolism, 1961
In 2 sisters, hyperthyroidism was associated with normal levels of serum protein-bound iodine (PBI). A decrease in thyroxine (T4) binding by serum alpha-globulin (TBG) and pre-albumin (TBPA) was demonstrated in both cases by paper electrophoresis in ammonium carbonate buffer. TBG capacities were 0.08 and 0.11 μg. of T4 per ml., and the serum PBI levels
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The Thyroxine-Binding Properties of Rat and Rabbit Serum Proteins

Endocrinology, 1976
The thyroxine (T4) binding properties of rat and rabbit serum proteins were studied using a gel equilibration technique, gel filtration and polyacrylamide gel electrophoresis. In both species two different T4 binding molecules were identified in whole serum and in Cohn fraction V preparations.
R L, Sutherland, M R, Brandon
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THYROXINE BINDING PROTEINS OF MOUSE SERUM AT PHYSIOLOGICAL pH

Acta Endocrinologica, 1969
ABSTRACT The binding properties of mouse serum for L-3'5'3,5 tetraiodothyronine (T4) and L-3'3,5, triiodothyronine (T3) were investigated by agar gel electrophoresis in several buffer systems at pH 7.4 and pH 8.6. Mouse serum binds T4 and T3 in the albumin and the α-globulin regions; these were designated as mouse thyroxine binding albumin (TBA)
A, Gordon, T, Coutsoftides
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