Ovigyn – somatropin is a human growth hormone, and is produced by recombinant DNA technology. By its structure, it absolutely does not differ in any way from the pituitary human growth hormone. The somatotropin molecule consists of one polypeptide chain, which in turn contains 190-191 amino acid residues (molecular weight about 22 thousand) with a mass of 22125 daltons. According to its chemical structure, physico-chemical and biological parameters, somatotropin is very similar to prolactin and placental lactogen, which was the reason for uniting them into one family. It is generally accepted that during evolution, these three hormones are derived from a single predecessor.
At the moment, the primary structure of human somatotropin and some animal species has already been established. Somatotropins belonging to different species have differences in the consecutive arrangement of amino acids, can have a clear structural homology between themselves. Each of them contains one residue of tryptophan and four residues of cysteine. The cysteine residues take part in the formation of two disulfide bridges in the molecule, which then form 2 loops: the 1st largest – includes the central portion of the amino acid sequence (in the human somatotropin, it occupies the site between cysteine-54 and cysteine-165), and 2 -I small (at the C-terminal site between cysteine-182 and cysteine-189). A molecule of somatotropin with a spatial structure is an ordered character. In the polypeptide chain of human somatotropin, 4a-helices and 3 non-regular patches were found.
In general, human somatotropin has a number of differences from somatropines in animals by 34-35% (somatotropins of animals do not show activity when ingested, and human somatotropins on the contrary become active when ingested in an animal’s blood).