title: (A14-phenylalanine)insulin: a new synthetic analogue.
abstract: An analogue of porcine insulin which differs from the native molecule in that the amino acid residue A14-tyrosine is replaced by phenylalanine has been synthesized. The [PheA14]A chain was synthesized by the fragment condensation method and purified as tetra-S-sulfonate by ion-exchange chromatography on DEAE-cellulose at pH 5.6. Conversion of the tetra-S-sulfonate A chain to the sulfhydryl form and combination with native porcine sulfhydryl B chain gave the [PheA14]insulin, which was purified by gel filtration and ion-exchange chromatography on DEAE-cellulose. The biological activity of this analogue was 96 +/- 6% as measured by the rat epididymal adipocytes. This shows that A14-tyrosine is not essential for the biological activity of the hormone.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D007328:Insulin / Q000031:analogs & derivatives* / Q000138:chemical synthesis; D008297:Male; D051381:Rats; D013329:Structure-Activity Relationship; D013552:Swine; D014443:Tyrosine
chemical_list: D007328:Insulin; D014443:Tyrosine; C027603:insulin, Phe(A14)-