Molecular weight analysis of isopenicillin N synthase by electrospray mass spectrometry

FEBS Letters

Baldwin, J.E.¹  Aplin, R.T.¹  Fujishima, Y.¹  Jarvis, S.A.²  Schofield, C.J.¹  Green, B.N.² 

[1] The Dyson Perrins Laboratory and the Oxford Centre or Molecular Sciences, South Parks Road, Oxford 0X1 3QY UK;VG Mass Lab Ltd, Tudor Road, Altrincham, Cheshire WA14 5RZ, UK

关键词: Cephalosporium acremonium;    Electrospray mass spectrometry;    Isopenicillin N synthase;    Molecular weight;    Penicillin biosynthesis;   

DOI  :  10.1016/0014-5793(90)80251-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The use of electrospray mass spectrometry as a tool in analytical biochemistry was illustrated by determination of the molecular weights of wildtype and recombinant isopenicillin N synthase (IPNS). The molecular weight of recombinant IPNS produced using an expression system which generated soluble protein was found to be between 38 364 and 38 376 Da, ca 60 mass units higher than that of the wildtype material, consistent with the presence of an additional N-terminal glycine in the former. Observed molecular weights were all ca 70 Da higher than that calculated from sequence information, consistent with the complexion of a partially hydrated iron atom to the enzyme during analysis.

【 授权许可】

Unknown