Properties of proteins binding plasma progesterone in pregnant Cape porcupines (Hystrix africaeaustralis)

Louw, Abraham I.; Wyk, V. van; Aarde, Rudi J. van

doi:10.1530/jrf.0.0960117

Cited by 5 publications

(1 citation statement)

References 21 publications

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“…The LBD‐ER immobilised MNPs were then boiled at 100°C for 5 min to denature the LBD‐ER protein, thus releasing the bound compounds. The content of bound compounds was determined by measuring the absorbance at 280 nm, commonly used to determine the relative contents of E2, P4 and phytoestrogens [25, 26].…”

Section: Methodsmentioning

confidence: 99%

Simple assay for screening phytoestrogenic compounds using the oestrogen receptor immobilised magnetite nanoparticles

Busayapongchai

Siri

2016

IET nanobiotechnol.

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With increasing interests of phytoestrogens for their potential applications, a rapid and simple tool for screening these phytochemicals is still required. In this study, a simple assay to detect phytoestrogens was developed based on the competition binding between the tested samples and the fluorescently labelled oestrogen (E2) to the human ligand binding domain of oestrogen receptor (LBD-ER) that was immobilised on the magnetite nanoparticles (MNPs). The 40-kDa LBD-ER peptide was produced in an system. The synthesised 68.7-nm MNPs were silanised and subsequently covalently linked to the C-terminus of LBD-ER peptide. The LBD-ER immobilised MNPs demonstrated the specific binding for the standard E2 with the equilibrium dissociation constant of 9.56 nM and the binding capacity of 0.08 pmol/1 mg of the MNPs. The LBD-ER immobilised MNPs could evaluate oestrogenic activity of the extracts of and , the reported phytoestrogenic plants, but not progesterone (P4) and extract, the negative controls. The results of this work clearly demonstrated a potential assay for detecting phytoestrogens of crude plant extracts, which is simple and easily adapted to a high throughput format.

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Section: Methodsmentioning

confidence: 99%