PMID: 6381277May 1, 1984

Isolation and amino-acid sequence determination of monkey insulin and proinsulin

Hoppe-Seyler's Zeitschrift für physiologische Chemie
V K NaithaniD F Steiner


Insulin has been isolated and purified from rhesus monkey pancreas by means of acid-ethanol extraction, gel filtration and ion exchange chromatography. The complete amino-acid sequence of the hormone has been determined by amino-acid analysis of the oxidized A- and B-chains, by end group determination, by the identification of the C-terminal residues (AsnA21 and ThrB30) by carboxypeptidase A digestion and by Edman degradation of the S-carboxymethylated A- and B-chains. The 51-residue monkey insulin was shown to be identical to human insulin. From the known insulin and C-peptide sequence the primary sequence of monkey proinsulin has been proposed.


Jul 8, 1999·Proceedings of the National Academy of Sciences of the United States of America·N S KenyonC Ricordi
May 15, 1986·Archives of Biochemistry and Biophysics·G HalldénH Jörnvall
Feb 14, 2007·American Journal of Physical Anthropology·Diana S Sherry, Peter T Ellison
Jul 17, 2003·The Journals of Gerontology. Series A, Biological Sciences and Medical Sciences·Theresa A GreslJoseph W Kemnitz
Sep 1, 1987·International Journal of Peptide and Protein Research·T MajewskiJ Markussen


Feb 1, 1967·Proceedings of the National Academy of Sciences of the United States of America·D F Steiner, P E Oyer

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