Competitive Ligand-Binding Assay for Measurement of Sex Hormone-Binding Globulin (SHBG)

1973 ◽  
Vol 37 (6) ◽  
pp. 873-881 ◽  
Author(s):  
DAN TULCHINSKY ◽  
INDER J. CHOPRA
1984 ◽  
Vol 58 (4) ◽  
pp. 619-628 ◽  
Author(s):  
INDER J. CHOPRA ◽  
TIEN-SHANG HUANG ◽  
ROBERT E. HURD ◽  
ANGELITA BEREDO ◽  
DAVID H. SOLOMON

1975 ◽  
Vol 80 (1_Suppla) ◽  
pp. S15
Author(s):  
K. H. Rudorff ◽  
H. J. Kröll ◽  
J. Herrmann

Author(s):  
J A Whittaker ◽  
M L Cawood ◽  
R E Oakey

A binding assay for sex hormone binding globulin (SHBG) has been developed in which SHBG is saturated with tritiated dihydrotestosterone (DHT). Separation of bound and free DHT is achieved by using Concanavalin A-Sepharose as a solid phase matrix. The method is described and its performance, including linearity, imprecision and comparison with other methods, is assessed. The assay is simple and robust and is suitable for analysis of samples of plasma or serum for clinical or research use.


1997 ◽  
Vol 52 (11-12) ◽  
pp. 834-843 ◽  
Author(s):  
Matthias Schöttner ◽  
Dietmar Ganßer ◽  
Gerhard Spitelle

Abstract Lignans bind to sex hormone-binding globulin (SHBG ). The lignan with the highest binding affinity is (±)-3,4-divanillyltetrahydrofuran. In a double Stobbe condensation - without use of protecting groups - a wide variety of lignans with different substitution pattern in the aromatic and aliphatic part of the molecule was synthesized. These lignans were tested in a SHBG -binding assay which allowed to deduce the following relationship between structure and activity: 1) (±)-diastereoisomers are more active than meso compounds 2.) the 4-hydroxy- 3-methoxy (guajacyl) substitution pattern in the aromatic part is most effective 3.) the activity increases with the decline in polarity of the aliphatic part of the molecule.


Steroids ◽  
2003 ◽  
Vol 68 (7-8) ◽  
pp. 629-639 ◽  
Author(s):  
Hagen Hauptmann ◽  
Jochen Metzger ◽  
Andreas Schnitzbauer ◽  
Claude Y Cuilleron ◽  
Elisabeth Mappus ◽  
...  

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