An insulin fragment, representing the C-terminal functionally important sit
e of its molecule and responsible for receptor binding, was synthesized. Th
e fragment consists of two peptides: a dipeptide (A 20-21) and an octapepti
de (B 19-26), linked with a disulfide bond (A20 - B19), The biological acti
vity of the newly synthesized fragment relative to insulin was assayed for
the influence on glycogenesis and for the ability to stimulate glucose upta
ke. Comparative tests for the biological activity of the synthesized fragme
nt and of the intact hormone allowed us to conclude that the fragment has i
nsulin-like properties.