Chaga G, Andersson L, Porath J
Biochemical Separation Centre, Uppsala University, Sweden.
J Chromatogr. 1992 Dec 25;627(1-2):163-72. doi: 10.1016/0021-9673(92)87196-f.
Lactate dehydrogenase from chicken breast muscle was purified to homogeneity in one step by immobilized metal ion affinity chromatography. The purified enzyme was used to localize the binding site to immobilized Fe(III) ions. After cyanogen bromide degradation and digestion with trypsin, small enzyme fragments capable of binding to immobilized Fe(III) ions were obtained. It is proposed that several histidyl groups are involved in the binding.
