scholarly journals Modulation of High Affinity Hormone Binding

1998 ◽  
Vol 273 (11) ◽  
pp. 6285-6291 ◽  
Author(s):  
KiSung Ryu ◽  
HunYoung Lee ◽  
SooPyung Kim ◽  
Jeremy Beauchamp ◽  
Chang-Shung Tung ◽  
...  
1982 ◽  
Vol 100 (1) ◽  
pp. 120-130
Author(s):  
Oscar A. Lea

Abstract. The binding of 5α-dihydroprogesterone (DHP)1 to proteins in pregnancy serum has been investigated and compared with the binding of progesterone. Characteristic properties of the DHP-serum protein interaction were unsaturability, low affinity and poor complex stability. Fractionation of serum using a variety of protein separation techniques, revealed that DHP interacts with several proteins. At low temperature (0–4°C) albumin appeared to be the principal binding component whereas higher temperatures seemed to favour binding to β-lipoproteins and α2-macroglobulin. Binding to specific binding proteins such as the corticosteroid binding globulin (CBG) and the sex hormone-binding globulin, (SHBG) were detectable but appeared to be quantitatively unimportant. Progesterone showed a similar multicomponent interaction but differed from DHP in the extent of binding to CBG. Binding of either hormone to the α1-acid-glycoprotein was negligible. The present study shows that the high endogenous DHP levels present in pregnancy sera are caused by factors other than high affinity protein binding.


2004 ◽  
Vol 36 (Supplement) ◽  
pp. S239
Author(s):  
Duncan N. French ◽  
Martyn R. Rubin ◽  
William J. Kraemer ◽  
Carl M. Maresh ◽  
Jeff S. Volek ◽  
...  

1992 ◽  
Vol 37 (4) ◽  
pp. 373-378 ◽  
Author(s):  
C. A. M. Roelen ◽  
G. H. Donker ◽  
J. H. H. Thijssen ◽  
H. P. F. Koppeschaar ◽  
M. A. Blankenstein

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