コイ血漿アルブミンのmethemalbumin形成能およびヘマチン結合能

概要

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Two albumin components (S2 and S3E2) exhibiting methemalbumin(MHA)-forming ability were highly purified by a method essentially consisting of ammonium sulfate fractionation, Sephadex gel filtration, and starch grain electrophoresis. The MHA-forming ability of both components, especially of S3E2, was significantly stronger than that of human albumin. The hematin-binding ability of component S2 was clearly superior to that of S3E2. When methemoglobin (metHb) was added to various concentrations to the equimolar mixtures of both components, S3E2 formed preferentially MHA until the equimolar level was reached, and beyond this level component S2 also began to form MHA. The order of manifestation of their hematin-binding ability was the opposite: Component S2 preferentially bound hematin, while S3E2 also bound hematin only when hematin was present in a great excess.
公益社団法人日本水産学会の論文