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Studies on manganese complexes of human serum albumin

✍ Scribed by B.E. Chapman; T.E. MacDermott; W.J. O'Sullivan

Publisher
Elsevier Science
Year
1973
Weight
734 KB
Volume
3
Category
Article
ISSN
0006-3061

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✦ Synopsis

Proton relavstion rate studies of the interaction between manganous ion and human serum albumin indicated the presence of two equivalent sites for the binding of the metal ion to the protein. The enhancement, 61, of the binary Mn-HSA complex was determined to he 10.3 with a dissociation constant, KD of 60 pX_ Defatting of the HSA resulted in an increased value of l I to 18.0 and KD of 130 &f. Subsequent formation of the copper (1: 1)

and chromium (average 1.5 : 1) complexes of HSA had no significant effect on the biding of t.he manganous ion.

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