Modified high-affinity binding of Ni2+, Ca2+ and Zn2+ to natural mutants of human serum albumin and proalbumin.

doi:10.1042/bj3010217

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Article

Modified high-affinity binding of Ni2+, Ca2+ and Zn2+ to natural mutants of human serum albumin and proalbumin.

The Biochemical journal - 1 Jul 1994

Kragh-Hansen U, Brennan S O, Minchiotti L, Galliano M

Abstract excerpt

High-affinity binding of radioactive Ni2+, Ca2+ and Zn2+ to six genetic albumin variants and to normal albumin isolated from the same heterozygote carriers was studied by equilibrium dialysis at pH 7.4. The three cations bind differently to albumin. Ni2+ binds to a site in the N-terminal region o...

Topics

Amino Acid Sequence
Binding Sites
Calcium
Genetic Variation
Humans
In Vitro Techniques
Kinetics
Mutation
Nickel
Prealbumin
Protein Binding
Serum Albumin
Zinc

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