Five albumin components designated S
2D
1, S
2D
2, S
3E
1, S
3E
2, and S
3E
3, were isolated from carp plasma by a combination of Sephadex G-200 gel Filtration, DEAE-cellulose column chromatography, and preparative electrophoresis. Their molecular weights, in the above order, were estimated to be 145, 000, 145, 000, 58, 000, 71, 000, and 71, 000, respectively. It was demonstrated that each of components S
2D
1 and S
2D
2 is composed of several subunit chains, while each of the remaining components constitutes a single chain. Results of the dye binding tests showed that only components S
2D
1 and S
2D
2 bin with BPB, though all five components bind with HABA and BCG. Component S
3E
2 showed the strongest BCG-binding ability. All the components except S
3E
1 exhibited methemalbumin forming ability. Components S
3E
1 and S
3E
2 showed Sevin esterase activity. It was noted that component S
3E
2 is highest in these activities.
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