Identification by fast atom bombardment mass spectrometry of insulin fragments produced by insulin proteinase

We describe the isolation by reversed-phase h.p.l.c. of a number of products of the degradation of insulin by insulin proteinase and their direct analysis by fast atom bombardment mass spectrometry (f.a.b.-m.s.). Various semisynthetically labelled insulins were used, including [[2H2]GlyA1]insulin an...

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Veröffentlicht in:Biochemical journal 1988-01, Vol.249 (1), p.215-222
Hauptverfasser: Savoy, L A, Jones, R M, Pochon, S, Davies, J G, Muir, A V, Offord, R E, Rose, K
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Sprache:eng
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Zusammenfassung:We describe the isolation by reversed-phase h.p.l.c. of a number of products of the degradation of insulin by insulin proteinase and their direct analysis by fast atom bombardment mass spectrometry (f.a.b.-m.s.). Various semisynthetically labelled insulins were used, including [[2H2]GlyA1]insulin and [18O]LysB29]insulin. The results obtained confirm and extend the results obtained by non-mass-spectrometric methods [Davies, Muir, Rose & Offord (1988) Biochem. J. 249, 209-214, and papers cited therein]. Cleavage sites were identified between positions A13-A14, A14-A15, B9-B10, B13-B14, B24-B25 and B25-B26. The advantages and disadvantages of the application of f.a.b.-m.s. to such studies are discussed.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2490215