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Structure-function studies on gastrointestinal hormones: I. Synthesis of secretin analogs and their biological and immunological properties

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Schulz,  Irene
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Moroder, L., Jaeger, E., Drees, F., Gemeiner, M., Knof, S., Stelzel, H.-P., et al. (1980). Structure-function studies on gastrointestinal hormones: I. Synthesis of secretin analogs and their biological and immunological properties. Bioorganic Chemistry, 9(1), 27-54. doi:10.1016/0045-2068(80)90031-0.


Cite as: https://hdl.handle.net/21.11116/0000-0008-40FC-4
Abstract
Syntheses by conventional procedures of the three analogs corresponding to the porcine secretin sequence crossed at position 6 by the N-terminal hexapeptide sequences of VIP, GIP, and glucagon are described, viz., Ala4,Val5-, Tyr1,Ala2,Glu3-, and Gln3-secretin (VIP-SN, GIP-SN, and GLU-SN). The analog Phe1,Phe2,Trp3,Lys4-secretin (SOMA-SN), designed on the basis of the surprising homology of the sequence portions 10–13 of somatostatin and 5–8 of secretin, was also prepared. Finally, the synthesis of Nα-3-(4-hydroxyphenyl)propionyl-β-alanyl-secretin (DATA-SN), a tracer suitable for secretin radioimmunoassay and as an N-terminus modified secretin analog, is reported. The analogs are compared, in terms of their biological and immunological properties in different assay systems, with pure synthetic secretin.