Identification of radioactive insulin fragments liberated by insulin proteinase during the degradation of semisynthetic [3H]GlyA1]insulin and [3H]PheB1]insulin.
(1) We [Muir, Offord & Davies (1986) Biochem. J. 237, 631-637 and Davies, Muir & Offord (1986) Biochem. J. 240, 609-612] have previously identified a major product in the degradation of insulin by insulin proteinase (the N-terminal fragment produced by cleavage between residues LeuA13 and TyrA14, SerB9 and HisB10) together with evidence for a minor cleavage site between HisB10 and LeuB11 or between LeuB11 and ValB12. (2) We now present evidence for minor sites of cleavage between TyrA14 and GlnA15, GluB13 and AlaB14 as well as HisB10 and LeuB11.
Davies
J G
JG
Département de Biochimie Médicale, Centre Médical Universitaire, Geneva, Switzerland.
Muir
A V
AV
Rose
K
K
Offord
R E
RE
D002851:Chromatography, High Pressure Liquid; D004590:Electrophoresis, Paper; D007328:Insulin / Q000031:analogs & derivatives*; D007339:Insulysin; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis*; D010447:Peptide Hydrolases; D014316:Tritium
D007328:Insulin; D010446:Peptide Fragments; C054928:insulin, Gly(A1)-; C054929:insulin, Phe(B1)-; D014316:Tritium; D010447:Peptide Hydrolases; D007339:Insulysin