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Mass spectrometry copper binding

The study of these peptides and their copper and zinc complexes by mass spectrometry revealed much information about their composition and binding characteristics. The most interesting results were those from the study of patellamide C and its copper complexes. This revealed the formation of complexes, such as [PatCH2 + 2Cu + (CsHsOs)] which were not detected by CD. This species might be similar to the copper complex of ascidiacyclamide, which was shown by X-ray crystallography to have a bridging carbonate between the two copper atoms. ... [Pg.156]

Inagaki, K., Mikuriya, N., Morita, S., Haraguchi, H., Nakahara.Y, Hattori, M., Kinosita.T., and Saito, H. (2000). Speciation of protein-binding zinc and copper in human blood serum by chelating resin pre-treatment and inductively coupled plasma mass spectrometry. Analyst (London) 125,197—204. [Pg.226]

See other pages where Mass spectrometry copper binding is mentioned: [Pg.112]    [Pg.6097]    [Pg.142]    [Pg.247]    [Pg.50]    [Pg.178]    [Pg.6096]    [Pg.5]   
See also in sourсe #XX -- [ Pg.50 , Pg.57 ]



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