Isolation and amino-acid sequence determination of monkey insulin and proinsulin.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002096:C-Peptide / Q000032:analysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007328:Insulin / Q000032:analysis* / Q000302:isolation & purification; D008253:Macaca mulatta; D011384:Proinsulin / Q000032:analysis* / Q000302:isolation & purification
D002096:C-Peptide; D007328:Insulin; D011384:Proinsulin