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Science 12 July 1968:
Vol. 161. no. 3837, pp. 165 - 167
DOI: 10.1126/science.161.3837.165
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Articles

Porcine Proinsulin: Characterization and Amino Acid Sequence

Ronald E. Chance 1, Robert M. Ellis 1, and William W. Bromer 1

1 Lilly Research Laboratories, Indianapolis, Indiana 46206

Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly-Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)