کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1935369 1050663 2008 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Noncooperative cadmium(II) binding to human metallothionein 1a
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Noncooperative cadmium(II) binding to human metallothionein 1a
چکیده انگلیسی

The two-domain (βα) mammalian metallothionein binds seven divalent metals, however, the binding mechanism is not well characterized and recent reports require the presence of the partially metallated protein. In this paper, step-wise metallation of the metal-free, two-domain βα-rhMT and the isolated β-rhMT using Cd(II) is shown to proceed in a noncooperative manner by analysis of electrospray ionization mass spectrometric data. Under limiting amounts of Cd(II), all intermediate metallation states up to the fully metallated Cd3-β-rhMT and Cd7-βα-rhMT were observed. Addition of excess Cd(II), resulted in formation of the supermetallated (metallation in excess of normal levels) Cd4-β- and Cd8-βα-metallothionein species. These data establish that noncooperative cadmium metallation is a property of each isolated domain and the complete two-domain protein. Our data now also establish that supermetallation is a property that may provide information about the mechanism of metal transfer to other proteins.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 372, Issue 4, 8 August 2008, Pages 840–844
نویسندگان
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