An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I.
We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors.
Department of Biochemistry, Mount Sinai School of Medicine, New York, New York 10029-6574.
S
S
Joshi
G T
GT
Burke
P G
PG
Katsoyannis
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006801:Humans; D007328:Insulin / Q000138:chemical synthesis*; D007334:Insulin-Like Growth Factor I; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis; D051381:Rats; D012756:Sheep
D007328:Insulin; D010446:Peptide Fragments; D007334:Insulin-Like Growth Factor I