Structural features involved in the biological activity of insulin and the insulin-like growth factors: [formula omitted]

A synthetic insulin-like compound consisting of the A-chain of insulin extended at its carboxyl terminus with the hexapeptide “D-domain” of insulin-like Growth Factor II, linked via disulfide bonds to a B-chain corresponding to the “B-domain” of insulin-like Growth Factor I, has been examined for in...

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Published inBiochemical and biophysical research communications Vol. 133; no. 2; pp. 423 - 429
Main Authors Joshi, Satish, Ogawa, Hiroshi, Burke, G.Thompson, Tseng, Lucy Y-H., Rechler, Matthew M., Katsoyannis, Panayotis G.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 1985
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Summary:A synthetic insulin-like compound consisting of the A-chain of insulin extended at its carboxyl terminus with the hexapeptide “D-domain” of insulin-like Growth Factor II, linked via disulfide bonds to a B-chain corresponding to the “B-domain” of insulin-like Growth Factor I, has been examined for insulin-like metabolic activity and for mitogenic activity. The synthetic material ( A 27 insulin B IGF-I ) is less potent than insulin in metabolic assays, and less potent than both insulin and IGF-I in mitogenic assays. It is proposed that neither the “D-domain” nor the “B-domain” of the IGFs is a major contributor to mitogenic activity. Their presence in the same molecule does not result in significant growth-promoting activity.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)90923-4