Interactions of foetal steroid binding protein with other binding proteins in human serum

Forbes, A ORCID: https://orcid.org/0000-0001-7416-9843, Wilkinson, M L, Iqbal, M J and Williams, R (1987) Interactions of foetal steroid binding protein with other binding proteins in human serum. Clinica Chimica Acta, 169 (2-3). pp. 299-308. ISSN 0009-8981

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Abstract

Foetal steroid binding protein (FSBP) which is present in normal human serum sometimes exhibits unusual sex-steroid binding; its effects on steroid action are uncertain but potentially important in view of the different levels seen in populations at different risk of breast cancer. Studies of the binding of 5 alpha-dihydrotestosterone to FSBP were conducted at varying concentrations of human serum albumin (HSA) and sex hormone binding globulin (SHBG). The saturable, specific binding of purified FSBP (Ka approximately equal to 5 X 10(8) l/mol), was transformed to a rising, plateau pattern by the addition of HSA. In equilibrium dialysis, FSBP competed with HSA or SHBG in a strictly proportional way when the third protein was absent. In the presence of HSA an initial sharp shift of ligand from SHBG to FSBP was observed with increasing FSBP concentration, but this was reversed as higher levels were reached. Steroid binding by FSBP in vivo may be determined predominantly by its interactions with other binding proteins.

Item Type: Article
Uncontrolled Keywords: blood proteins,carrier proteins,dialysis,female,fetus,humans,male,pregnancy,protein binding,serum albumin,sex hormone-binding globulin,sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology
Faculty of Medicine and Health Sciences > Research Groups > Nutrition and Preventive Medicine
Depositing User: Pure Connector
Date Deposited: 06 Aug 2014 10:44
Last Modified: 24 Oct 2022 23:58
URI: https://ueaeprints.uea.ac.uk/id/eprint/49505
DOI:

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