Title : Alteration of nickel-binding proteins in nickel-resistant cells.

Pub. Date : 1989

PMID : 2702040






7 Functional Relationships(s)
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1 Wild-type cells contained three major nickel-binding proteins with molecular masses of 68 kDa (p68), 55 kDa (p55), and 48 kDa (p48). Nickel H3 histone pseudogene 44 Homo sapiens
2 Both the p55 and p48 proteins appeared to be present in similar amounts in wild-type and nickel-resistant cell lines, based upon silver staining of two-dimensional gels, yet in the nickel-resistant B200 cells, these proteins could not be visualized by [63Ni] binding. Nickel H3 histone pseudogene 44 Homo sapiens
3 Both the p55 and p48 proteins appeared to be present in similar amounts in wild-type and nickel-resistant cell lines, based upon silver staining of two-dimensional gels, yet in the nickel-resistant B200 cells, these proteins could not be visualized by [63Ni] binding. Nickel H3 histone pseudogene 44 Homo sapiens
4 Among the nickel-binding proteins studied, the p55 contained nickel-binding sites that were the most resistant to exchange by excess nickel ions. Nickel H3 histone pseudogene 44 Homo sapiens
5 Among the nickel-binding proteins studied, the p55 contained nickel-binding sites that were the most resistant to exchange by excess nickel ions. Nickel H3 histone pseudogene 44 Homo sapiens
6 Among the nickel-binding proteins studied, the p55 contained nickel-binding sites that were the most resistant to exchange by excess nickel ions. Nickel H3 histone pseudogene 44 Homo sapiens
7 The microsomal fraction that contained the highest concentration of p55 also had the highest nickel-binding activity when standardized for protein concentration. Nickel H3 histone pseudogene 44 Homo sapiens