PMID: 1069990Dec 1, 1976

Amino-terminal sequences of two polypeptides from human serum with nonsuppressible insulin-like and cell-growth-promoting activities: evidence for structural homology with insulin B chain

Proceedings of the National Academy of Sciences of the United States of America
E Rinderknecht, R E Humbel

Abstract

The amino-terminal sequences of two polypeptides with nonsuppressible insulin-like and cell-growth-promoting activities (NSILA I and II), isolated from human serum, were determined. Of the first 31 residues, 22 are identical in NSILA I and II. Moreover, a striking structural similarity was found between NSILA and insulin B chain: 47 and 57% of residues 1-30 in NSILA I are identical to those in insulin B chain from man and tuna fish, respectively. This high degree of sequence identity is presented as evidence for homology and thus for a common evolutionary origin of insulin and NSILA. Based on these results and on these results and on biological properties of NSILA described earlier, a new designation for NSILA is proposed: insulin-like growth factor (IGF).

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