An enzyme-linked immunosorbent assay for fetal steroid binding protein of human serum

Steroids ◽  
1985 ◽  
Vol 45 (1) ◽  
pp. 31-38 ◽  
Author(s):  
M. Jawed Iqbal ◽  
Alastair Forbes ◽  
Timothy P. Corbishley ◽  
Mark L. Wilkinson ◽  
Roger Williams
1987 ◽  
Vol 114 (4) ◽  
pp. 584-588 ◽  
Author(s):  
M. Jawed Iqbal ◽  
Alastair Forbes ◽  
Mark L. Wilkinson ◽  
John W. Moore ◽  
Roger Williams ◽  
...  

Abstract. In order to examine the newly-discovered sex-steroid binding protein, foetal steroid binding protein (FSBP) in different populations, its binding characteristics and its level were studied by two-tier column ligand binding assay and enzyme-linked immunosorbent assay (ELISA) respectively. In 10 Japanese premenopausal women, analysis of 5α-dihydrotestosterone (DHT) binding in the Cibacron Blue 3GA-Sepharose 6B portion of the column showed a rising plateau pattern with a mean maximum binding of 31.1 ± 7.41%, whereas of 9 similar British women, 8 displayed unsaturable, non-cooperative binding of 11.6 ± 8.22% (P < 0.01). After partial purification of FSBP in these samples, the protein exhibited saturable binding kinetics, median binding 25 (interquartiles 23–34) and 19 (13–25) nmol DHT/l in Japanese and British women, respectively (P < 0.05). By analyzing FSBP by ELISA in 56 Japanese (45 premenopausal) and 59 British (25 premenopausal) women, higher levels were obtained in the whole Japanese group (P = 0.0016) and in the premenopausal Japanese women (P = 0.018) than in their British counterparts. In both nationalities, FSBP levels were higher in premenopausal women, and there was a significant negative correlation of FSBP with age in both populations, particularly in postmenopausal women. FSBP levels did not correlate with weight, parity, sex hormone binding globulin or albumin levels. The influence of FSBP on free steroid levels remains unclear, but some relationship with ovarian function seems a possibility.


1987 ◽  
Vol 169 (2-3) ◽  
pp. 299-308
Author(s):  
Alastair Forbes ◽  
Mark L. Wilkinson ◽  
M.Jawed Iqbal ◽  
Roger Williams

Biochemistry ◽  
1975 ◽  
Vol 14 (5) ◽  
pp. 957-963 ◽  
Author(s):  
Kenneth E. Mickelson ◽  
Philip H. Petra

1986 ◽  
Vol 240 (1) ◽  
pp. 75-79 ◽  
Author(s):  
M L Wilkinson ◽  
M J Iqbal ◽  
A Forbes ◽  
T P Corbishley ◽  
R Williams

In order to develop an immunoassay for foetal steroid-binding protein in human serum, which is impossible to assay quantitatively in normal samples by conventional ligand-binding techniques, the protein was purified by salt precipitation, affinity chromatography and gel filtration. Elution was by competing ligand or alkaline pH. The purified protein was further characterized and a highly specific antiserum was raised in rabbits.


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