Characterization of Met-139 as the photolabeled amino acid residue in the steroid binding site of sex hormone binding globulin using .DELTA.6 derivatives of either testosterone or estradiol as unsubstituted photoaffinity labeling reagents

Biochemistry ◽  
1992 ◽  
Vol 31 (33) ◽  
pp. 7609-7621 ◽  
Author(s):  
Catherine Grenot ◽  
Arnaud De Montard ◽  
Thierry Blachere ◽  
Marc Rolland De Ravel ◽  
Elisabeth Mappus ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Photoaffinity Labeling ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Steroid Binding ◽  
Derivatives Of

Resolution of a Disordered Region at the Entrance of the Human Sex Hormone-binding Globulin Steroid-binding Site

2002 ◽  
Vol 318 (3) ◽  
pp. 621-626 ◽  
Author(s):  
Irina Grishkovskaya ◽  
George V Avvakumov ◽  
Geoffrey L Hammond ◽  
Yves A Muller
Keyword(s):  
Binding Site ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Steroid Binding

Characterization of sex hormone binding globulin ligands with potential to enhance sex steroid action

2018 ◽  
Author(s):  
Phillip Round ◽  
Samir Das ◽  
Kristiina Wahala ◽  
Petegem Filip Van ◽  
Geoffrey Hammond
Keyword(s):  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Sex Steroid ◽  
Hormone Binding

Binding of Testosterone and Oestradiol to Sex Hormone Binding Globulin, Human Serum Albumin and other Plasma Proteins: Evidence for Non-Specific Binding of Oestradiol to Sex Hormone Binding Globulin

1983 ◽  
Vol 64 (3) ◽  
pp. 307-314 ◽  
Author(s):  
M. Jawed Iqbal ◽  
Maureen Dalton ◽  
Robert S. Sawers
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Plasma Proteins ◽  
Specific Binding ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Normal Female ◽  
Hormone Binding

1. The percentage binding of testosterone (T) and oestradiol (E2) to sex hormone binding globulin (SHBG) and human serum albumin (HSA) was determined over a range of SHBG concentrations of 16–250 nmol of dihydrotestosterone (DHT) bound/l. It was found that the binding of both T and E2 to HSA was a function of their binding to SHBG and bore an inverse relationship to it. After removal of both SHBG and HSA from plasma by affinity chromatography a ‘residual’ binding of about 11% for T and 12% for E2 was still apparent. in addition to the specific high-affinity, low capacity binding of E2 to SHBG, non-specific low-affinity binding of 7–12% was demonstrated after selective denaturation of the specific binding site of the latter. 2. Competition studies indicated that although at the relatively higher levels of SHBG found in the normal female the physiological concentrations of E2, T and DHT need not be taken into account in estimating the unbound fractions of steroids, at the relatively lower levels of SHBG found in normal men and hirsute women, the physiological concentrations of T and DHT are effective in causing statistically significant displacement of E2 from the common, specific binding site on SHBG. 3. A simple computerized technique is described for the determination of fractions of E2 and T respectively, that are unbound to SHBG, unbound to SHBG and HSA, and unbound to all plasma proteins, when the total plasma levels of E2, T, DHT and SHBG are known.

Resolution of the steroid-binding and dimerization domains of human sex hormone-binding globulin by expression in Escherichia coli

Biochemistry ◽  
1995 ◽  
Vol 34 (10) ◽  
pp. 3231-3238 ◽  
Author(s):  
Catherine Hildebrand ◽  
Wayne P. Bocchinfuso ◽  
David Dales ◽  
Geoffrey L. Hammond
Keyword(s):  
Escherichia Coli ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Expression In Escherichia Coli ◽  
Steroid Binding
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