Massspectrometric analyses of transmembrane proteins in human erythrocyte membrane

Yoshito Abe, Tomohito Chaen, Xiu Ri Jin, Tomohiro Hamasaki, Naotaka Hamasaki

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


It is difficult to understand the functional mechanisms of integral membrane proteins without having protein chemical information on these proteins. Although there have been many attempts to identify functionally important amino acids in membrane proteins, chemically and enzymatically cleaved peptides of integral membrane proteins have been difficult to handle because of their hydrophobic properties. In the present study, we have applied an analytical method to transmembrane proteins combining amino acid sequencing, matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry, and liquid chromatography with electrospray ionization (LC/ESI) mass spectrometry. We could analyze most (97%) of the tryptic fragments of the transmembrane domains of band 3 as well as other minor membrane proteins. The peptide mapping of the transmembrane domain of band 3 was completed and the peptide mapping information allowed us to identify the fragments containing lysine residues susceptible to 4-acetamido-4′-isothiocyanatostilbene-2, 2′-disulfonic acid (SITS) and to 2,4-dinitrofluorobenzene (DNFB). This method should be applicable to membrane proteins not only in erythrocyte membranes but also in other membranes.

Original languageEnglish
Pages (from-to)97-106
Number of pages10
JournalJournal of biochemistry
Issue number1
Publication statusPublished - Jul 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Medicine(all)


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