Biomics

In the last decade, significant progress has been made in the study of plant analogues of mammalian and human hormones. If, just as it happens in an animal cell, these compounds act as regulators of metabolism, the question arises about the existence of receptors for them and there is a need to study the mechanisms of intracellular signaling. With help of affinity sorbent with immobilized thyroxine presumably take part in the reception of plant analogues of iodothyronines compounds were isolated from bean seedlings. The procedure of affinity isolation of receptors to the plant analogue of thyroxine with subsequent determination of the concentration of triiodothyronine in the isolated fractions was repeated 15 times (n=15). It was assumed that the concentration of binding sites of thyroxine analogues is equal to the concentration of the hormone determined in the sample by enzyme immunoassay, thus, it was assumed that the hormone binding sites were fully loaded. The calculation of the average concentration of binding sites in samples and absolute errors was carried out using the program Statistica for Windows version 10. The average number of iodothyronine (A) binding sites in picomoles per 1 gram of raw tissue mass (pmol/g) was calculated using the formula A= (C*V)/m, where C is the average concentration of thyroxine binding sites in mmol/l determined by enzyme immunoassay, V is the volume of the eluted fraction, m is the weight of the bean sprouts in grams. It is shown that the isolated compound is a nucleoprotein with a nucleic acid content of about 11% and contains binding sites not only of thyroxine, but also of steroid hormones.

plant thyroxine analog, intracellular receptor, affinity isolation, ribonucleoproteins

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