scholarly journals The rational use of mass spectrometry for amino acid sequence determination in peptides and extension of the possibilities of the method

FEBS Letters ◽  
1970 ◽  
Vol 7 (1) ◽  
pp. 8-12 ◽  
Author(s):  
M.M. Shemyakin ◽  
Yu.A. Ovchinnikov ◽  
E.I. Vinogradova ◽  
A.A. Kiryushkin ◽  
M.Yu. Feigina ◽  
...  
1983 ◽  
Vol 215 (2) ◽  
pp. 261-272 ◽  
Author(s):  
K Rose ◽  
M G Simona ◽  
R E Offord

A new technique is described that permits the permethylation of acylated peptides at the 2-10 nmol level. The presence of up to 400 micrograms of sodium dodecyl sulphate per sample does not affect the reaction yields. The technique, which is a miniaturization of the widely used methyl iodide/dimethylsulphinyl carbanion procedure, employs a layer of hexane to exclude moisture and oxygen from the reaction mixture. Analysis of the peptide derivatives by combined g.l.c.-mass spectrometry permits amino acid sequence information to be obtained. In addition to studies of digests of a model substrate (glucagon), the new permethylation technique has been used to identify a peptide of interest from a digest of a cytochrome and to define the N-termini of two proteins at the 5 nmol level.


1996 ◽  
Vol 225 (1) ◽  
pp. 146-150 ◽  
Author(s):  
Evelyn C. Ilg ◽  
Heinz Troxler ◽  
Daniel M. Bürgisser ◽  
Thomas Kuster ◽  
Michèle Markert ◽  
...  

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