MOLECULAR-WEIGHT ANALYSIS OF ISOPENICILLIN-N SYNTHASE BY ELECTROSPRAY MASS-SPECTROMETRY

被引：13

作者：

APLIN, RT

BALDWIN, JE

FUJISHIMA, Y

SCHOFIELD, CJ

GREEN, BN

JARVIS, SA

机构：

[1] DYSON PERRINS LAB,S PARKS RD,OXFORD OX1 3QY,ENGLAND

[2] OXFORD CTR MOLEC SCI,OXFORD OX1 3QY,ENGLAND

[3] VG MASS LAB LTD,ALTRINCHAM WA14 5RZ,CHESHIRE,ENGLAND

来源：

FEBS LETTERS | 1990年 / 264卷 / 02期

关键词：

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

D O I：

10.1016/0014-5793(90)80251-D

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. © 1990.

引用

页码：215 / 217

页数：3

共 15 条

[1] N-TERMINAL AMINO-ACID SEQUENCE AND SOME PROPERTIES OF ISOPENICILLIN-N SYNTHETASE FROM CEPHALOSPORIUM-ACREMONIUM [J].