サケ・トランスフェリンの精製と物理化学的性状

概要

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Transferrin (Tf) was isolated from serum of the chum salmon Oncorhynchus keta by neans of salting-out with ammonium sulfate, chromatography on DEAE-cellulose, starch block electrophoresis and gel filtration. The purified Tf showed a molecular weight of 84, 000 by gel filtration, 80, 000 by SDS-PAGE and 70, 000 by sedimentation equilibrium method. The sedimentation coefficient (S020, W) and the isoelectric point (pI) of the Tf were 5.31 and 5.3, respectively. N-terminal amino acid was identified to be alanine. The amino acid composition was also determined. The visible absorbent spectrum of the chum salmon Tf revealed the maximum absorption at 410 nm. The iron binding capacity of the Tf was estimated to be two atoms per molecule. The Tf represented 936-16.8% of the serum protein in the chum salmon. The immunological cross-reac-tivity between the Tf of chum salmon and that of 12 other fishes was tested. Tfs from the family Salmonidae revealed cross-reactivity.
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