Title : The exchange of Fe3+ between acetohydroxamic acid and transferrin. Spectrophotometric evidence for a mixed ligand complex.

Pub. Date : 1982 Jul 10

PMID : 7085638






4 Functional Relationships(s)
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Protein Name
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1 The velocity-concentration relationship shows a hyperbolic dependence on acetohydroxamic acid concentration and a linear dependence of Fe3+-transferrin-CO3(2-), suggesting a rate-limiting labilization of the Fe3+ of Fe3+-transferrin-CO3(2-) resulting from a conformational change. co3 transferrin Homo sapiens
2 The velocity-concentration relationship shows a hyperbolic dependence on acetohydroxamic acid concentration and a linear dependence of Fe3+-transferrin-CO3(2-), suggesting a rate-limiting labilization of the Fe3+ of Fe3+-transferrin-CO3(2-) resulting from a conformational change. co3 transferrin Homo sapiens
3 The velocity-concentration relationship shows a hyperbolic dependence on acetohydroxamic acid concentration and a linear dependence of Fe3+-transferrin-CO3(2-), suggesting a rate-limiting labilization of the Fe3+ of Fe3+-transferrin-CO3(2-) resulting from a conformational change. co3 transferrin Homo sapiens
4 The velocity-concentration relationship shows a hyperbolic dependence on acetohydroxamic acid concentration and a linear dependence of Fe3+-transferrin-CO3(2-), suggesting a rate-limiting labilization of the Fe3+ of Fe3+-transferrin-CO3(2-) resulting from a conformational change. co3 transferrin Homo sapiens