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Disulfide bond formation between the N‐terminal region of p56lck and the cytoplasmic domain of CD8 studied by Electrospray Ionization and Matrix‐Assisted Desorption/Ionization time‐of‐flight mass spectrometry
Author(s) -
Yi GwanSu,
Cheong Chaejoon
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201912
Subject(s) - chemistry , mass spectrometry , electrospray ionization , dimer , electrospray , monomer , ionization , crystallography , ion , analytical chemistry (journal) , chromatography , organic chemistry , polymer
Masses of the complexes formed between the C‐terminal region of CD8α (CD8αC) and the N‐terminal region of p56lck (p56lckN) were measured by using Electrospray Ionization (ESI) and Matrix‐Assisted Laser Desorption/Ionization (MALDI) Mass Spectrometry (MS). The two peptides were incubated with various metal ions, Zn++, Cd++, Co++, Fe++ and Ca++. The complex formed from the incubation did not contain any metal ions. Instead, its mass suggested that the complex was formed by two disulfide bonds. The fact that the incubation of the complex with Dithiothreitol broke the complex confirmed into monomers that the complex was formed through disulfide bonds. The only disulfide‐mediated complex formed was hetero‐dimer (CD8αC‐p56lckN) and none of homo‐dimers (CD8αC‐CD8αC or p56lckN‐p56lckN) were observed from ESI and MALDI‐TOF mass spectrometry.