[Genetic engineering in the bacterial synthesis of somatostatin].

Series of recombinant plasmids for expression of the synthetic gene somatostatin-14 (SST) as a fusion protein were obtained. The somatostatin gene was fused to chloramphenicol acetyltransferase (cat) or its deleted variant genes. Both parts of the resultant fusion protein were joined through a Met residue.

[Synthesis of somatostatin in Escherichia coli cells: isolation and characteristics].

A synthetic gene coding for somatostatin-14 (SST) was cloned in plasmid expression vectors in frame with the chloramphenicol acetyl transferase (CAT) gene, both genes being divided by a Met residue. The hybrid gene was expressed under the control of the CAT gene promoter (Pcat) or the tryptophan operon promoter (Ptrp). Them fused genes gave insoluble polypeptide products amounting from 5% of the total cellular protein under constitutive biosynthesis conditions (Pcat) to 30% upon induction (Ptrp).

Involvement of proteolytic enzymes in the lipotropic effect of the pituitary polypeptide hormones.

The influence of proteinase inhibitors on the lipolytic effect of the pituitary polypeptide hormones and epinephrine in an isolated adipose tissue of rabbits and rats has been studied. Neither of proteinase inhibitors changed the basal rate of lipolysis. Trasylol, a serine proteinase inhibitor, suppressed completely growth hormone (GH) effect and partially reduced the effect of adrenocorticotropin (ACTH) and beta-lipotropin (beta-LPH) but did not change the effect of epinephrine.

[New data on the biological activity of pituitary somatotropin fragment 77-107].

Some new evidence on the biological activity of somatotropin fragment 77-107 is given. This fragment was prepared from whale somatotropin by tryptic hydrolysis. Beside the previously established ability of the hormone to increase the width of the tibial epiphyseal cartilage in hypophysectomized rats ("tibia" test) two other properties of the fragment indicative of its growth-promoting activity were established.