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 in | Biochemical and biophysical research communications Vol. 133; no. 2; pp. 423 - 429 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
1985
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Subjects | |
Online Access | Get full text |
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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. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(85)90923-4 |