Steroid-binding proteins in rabbit plasma: Separation of testosterone-binding globulin (TeBG) from corticosteroid-binding globulin (CBG), preliminary characterization of TeBG, and changes in TeBG concentration during sexual maturation

1975 ◽  
Vol 2 (5) ◽  
pp. 351-368 ◽  
Author(s):  
Benjamin J. Danzo ◽  
Barbara C. Eller
1983 ◽  
Vol 19 ◽  
pp. 136
Author(s):  
H.J. Grill ◽  
A. Knichel ◽  
G. Schweikhart ◽  
T. Beck ◽  
B. Manz ◽  
...  

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.


1985 ◽  
Vol 75 (5) ◽  
pp. 823-829 ◽  
Author(s):  
Mark S. Langley ◽  
Geoffrey L. Hammond ◽  
Alan Bardsley ◽  
Ronald A. Sellwood ◽  
David C. Anderson

1978 ◽  
Vol 76 (1) ◽  
pp. 21-31 ◽  
Author(s):  
M. T. VU HAI ◽  
E. MILGROM

SUMMARY The synthetic progestogen R5020 (17,21-dimethyl-19-norpregna-4,9-diene-3,20-dione) binds with high affinity (Ka = 8·8 × 108 1/mol at 0 °C) to the progesterone receptor from rat uterine cytosol. At nanomolar concentrations, equilibrium is attained in less than 90 min. R5020 has a very low affinity for other specific steroid-binding proteins (corticosteroid-binding globulin and oestrogen receptors) present in relatively high concentrations in the uterine cytosol. The affinity of the receptor for the natural hormone progesterone is remarkably low (Ka= 1 × 108−1·7 × 1081/mol at 0 °C) which explains the instability of progesterone–receptor complexes. Advantage may be taken of this property to remove endogenous progesterone easily by charcoal treatment at 0 °C, a treatment which does not modify the concentration of receptors. A method based on these characteristics is described for the assay of the total number (progesterone-bound and unbound) of receptor sites in uterine cytosol. This assay may be used in various physiological situations where endogenous progesterone is present at unknown concentrations.


1985 ◽  
Vol 61 (1) ◽  
pp. 200-203 ◽  
Author(s):  
WILLIAM ROSNER ◽  
M. SAEED KHAN ◽  
CHARLES N. BREED ◽  
MARTIN FLEISHER ◽  
H. LEON BRADLOW

1988 ◽  
Vol 119 (1) ◽  
pp. 56-60 ◽  
Author(s):  
F. W. Chu ◽  
R. P. Ekins

Abstract. Corticosteroid binding globulin (CBG) was detected by a specific radioimmunoassay in mixed saliva (25.4 ± 4.0 μg/l, mean ± sem) and in pure, uncontaminated parotid fluids (17.4 ± 2.7 μg/l) at resting flowrates of approximately 500 μl/min and 50 μl/gland per min, respectively. In parotid fluids collected at stimulated flow-rates of between 300–1000 μl/gland per min, CBG could not be detected. This observation suggests the direct flow-rate-dependent transfer/secretion of CBG in saliva. When cortisol was measured (RIA) in dilution experiments in both mixed saliva and parotid fluids using phosphate buffer at pH 7.4 as diluent, a protein-binding effect analogous to that found in plasma samples was observed. However, this effect was abolished if a known CBG inhibitor, phosphate:citrate buffer at pH 4, was used as the diluent in the assay. A bound fraction of cortisol was found in both mixed saliva (14.0 ± 4.0%) and parotid fluid samples (12.3 ± 1.3%) by equilibrium dialysis. These findings appear to contradict the currently accepted notion that specific plasma steroid binding proteins, and hence the protein-bound steroids, are absent in uncontaminated saliva; and that their presence in mixed saliva is the consequence solely of contamination by gingival fluid and/or plasma from mouth or gum abrasions. We conclude that both protein-bound and free steroids are present in uncontaminated saliva and that salivary total and plasma free steroid concentrations are not identical.


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