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Anal Biochem. 1993 Oct;214(1):50-7.

Electrospray ionization mass spectrometry on hydrophobic peptides electroeluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis application to the topology of the sarcoplasmic reticulum Ca2+ ATPase.

Author information

1
Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.

Abstract

We describe a method to prepare proteins and peptides in a state suitable for exact determination of molecular mass by electrospray ionization mass spectrometry after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and electroelution. The utility of the procedure, in conjunction with N-terminal sequencing, in defining the C-terminal end of the peptide fragments produced by proteolysis of sarcoplasmic reticulum Ca2+ ATPase with V8 is demonstrated. The application of mass spectrometry aids significantly the use of proteolytic enzymes for topological studies of membrane proteins, and SDS-PAGE is preferable to reverse-phase HPLC for separation of membraneous, hydrophobic peptides and proteins.

PMID:
8250254
DOI:
10.1006/abio.1993.1455
[Indexed for MEDLINE]

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