A Method for the Determination of Sex Hormone Binding Globulin Using Concanavalin A-Sepharose

1992 ◽  
Vol 29 (2) ◽  
pp. 168-171 ◽  
Author(s):  
J A Whittaker ◽  
M L Cawood ◽  
R E Oakey
Keyword(s):  
Concanavalin A ◽  
Binding Assay ◽  
Solid Phase ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Research Use ◽  
Hormone Binding

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.

A method for the determination of sex hormone binding globulin in human serum

1985 ◽  
Vol 18 (5) ◽  
pp. 276-279
Author(s):  
Nannepaga Y. Zachariah ◽  
Rosalie V. Thornblom ◽  
Zaven H. Chakmakjian ◽  
Gardner G. Sumner
Keyword(s):  
Human Serum ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding

scholarly journals Interaction of Lignans with Human Sex Hormone Binding Globulin (SHBG)

1997 ◽  
Vol 52 (11-12) ◽  
pp. 834-843 ◽  
Author(s):  
Matthias Schöttner ◽  
Dietmar Ganßer ◽  
Gerhard Spitelle
Keyword(s):  
Binding Affinity ◽  
Binding Assay ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Protecting Groups ◽  
Hormone Binding ◽  
Substitution Pattern ◽  
Structure And Activity

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.

scholarly journals Characterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulin-like domain

1998 ◽  
Vol 330 (1) ◽  
pp. 389-396 ◽  
Author(s):  
Merel VAN WIJNEN ◽  
G. Jeanette STAM ◽  
T. G. Glenn CHANG ◽  
C. M. Joost MEIJERS ◽  
H. Pieter REITSMA ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Solid Phase ◽  
Anticoagulant Activity ◽  
Protein S ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Wild Type ◽  
Cofactor Activity

Protein S is a vitamin K-dependent glycoprotein involved in the regulation of the anticoagulant activity of activated protein C (APC). Also, an anticoagulant role for protein S, independent of APC, has been described. Protein S has a unique C-terminal sex hormone binding globulin (SHBG)-like domain that represents about half of the molecule. To define the role of this domain in APC cofactor activity and in binding to C4b-binding protein (C4BP), we have constructed a recombinant protein S molecule of N-terminal residues 1-242 that lacks the SHBG domain (mini-protein S). A panel of monoclonal antibodies directed against the N-terminal region of protein S recognized plasma-derived protein S, wild-type recombinant protein S and mini-protein S with similar affinities, whereas a monoclonal antibody that recognizes an epitope in the SHBG domain did not detect mini-protein S. Mini-protein S did not bind to C4BP in a solid-phase binding assay, and the cofactor activity of mini-protein S was not inhibited by preincubation with C4BP. In a plasma coagulation assay, the cofactor activity of mini-protein S was lower than wild-type or plasma-derived preparations. In contrast, no difference in APC cofactor activities was observed when the preparations were tested in purified systems that monitor the APC-mediated degradation of factors Va or VIIIa. In conclusion, we constructed a protein S molecule that fails to bind C4BP and still displays cofactor activity for APC. This confirms the role of the C-terminal SHBG region in C4BP binding and demonstrates that N-terminal residues 1-242 are sufficient for the expression of APC cofactor activity in a system using purified components. In plasma, however, the C-terminal SHBG region plays a role in the expression of optimal APC cofactor activity.

Levonorgestrel as a new radioligand for determination of sex hormone binding globulin in human plasma

Steroids ◽  
1983 ◽  
Vol 41 (4) ◽  
pp. 455-466 ◽  
Author(s):  
A.K. Srivastava ◽  
Anila Agnihotri ◽  
P. Tandon ◽  
V.P. Kamboj
Keyword(s):  
Human Plasma ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding

Effects of gonadotropin-releasing hormone on bioactivity of follicle-stimulating hormone (FSH) and microstructure of FSH, luteinizing hormone and sex hormone-binding globulin in a testosterone-based contraceptive trial: evaluation of responders and non-responders

1996 ◽  
Vol 135 (4) ◽  
pp. 433-439 ◽  
Author(s):  
Manuela Simoni ◽  
Jörg Peters ◽  
Hermann M Behre ◽  
Sabine Kliesch ◽  
Eckhard Leifke ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
Concanavalin A ◽  
Follicle Stimulating Hormone ◽  
Gonadotropin Releasing Hormone ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Molecular Heterogeneity ◽  
Hormone Binding ◽  
Releasing Hormone ◽  
Stimulating Hormone

Simoni M, Peters J, Behre HM, Kliesch S, Leifke E, Nieschlag E. Effects of gonadotropin-releasing hormone on bioactivity of follicle-stimulating hormone (FSH) and microstructure of FSH. luteinizing hormone and sex hormone-binding globulin in a testosterone-based contraceptive trial: evaluation of responders and non-responders. Eur J Endocrinol 1996;135:433–9. ISSN 0804–4643 Only a proportion of normal men participating in testosterone-based contraceptive trials develop azoospermia (responders). This study analyzed whether serum follicle-stimulating hormone (FSH), luteinizing hormone (LH) and sex hormone-binding globulin (SHBG) are qualitatively different between responders and non-responders. Determination of in vitro bioactive FSH after stimulation with gonadotropin-releasing hormone (GnRH) and analysis of molecular heterogeneity of serum FSH. LH and SHBG was carried out by chromatofocusing and concanavalin-A affinity chromatography in eight men who had participated in a previous contraceptive study with testosterone buciclate. Blood was withdrawn at 15-min intervals on two basal occasions and 30, 45 and 60 min after iv administration of GnRH (100 μg). Pools of sera were separated by chromatofocusing in the pH range 3–6 and by lectin chromatography on concanavalin A. Immunoreactive FSH, LH and SHBG were assayed in the eluates. Bioactive FSH was analyzed by the rat Sertoli cell bioassay. Serum bioactive FSH increased after GnRH stimulation, without significant differences between responders and non-responders. The chromatofocusing profiles of serum FSH showed a significant shift towards the less acidic region after GnRH. The isoform distribution was similar in responders and non-responders. No significant differences were found in the relative proportion of FSH, LH and SHBG retained by concanavalin A. It is concluded that the extent of suppression of sperm production by androgen administration cannot be foreseen either on the basis of the response of bioactive FSH to GnRH administration or from the glycosylation pattern of serum FSH, LH and SHBG. E Nieschlag, Institute of Reproductive Medicine of the University, Domagkstr. 11, D-48129 Münster, Germany

scholarly journals DETERMINATION OF SERUM SEX HORMONE BINDING GLOBULIN IN POLYCYSTIC OVARIAN SYNDROME & HEALTHY WOMEN

2019 ◽  
Vol 9 (4) ◽  
pp. 381-389
Author(s):  
Razaw O. Ibrahim ◽  
◽  
Shirwan H. Omer ◽  
Chro N. Fattah ◽  
◽  
...  
Keyword(s):  
Polycystic Ovarian Syndrome ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Healthy Women ◽  
Ovarian Syndrome
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