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Two parvalbumins from the muscle of the electric eel, Electrophorus electricus, were purified by Sephadex G-50 gel filtration followed by DE-52 ion exchange column chromatography. From 350g fresh eel muscle, 100—150mg of pure major component (Parvalbumin Ⅰ, PⅠ=4.25) can be isolated. The content of Parvalbumin Ⅱ is around one-fifth of the major one, and its pⅠ is 3.85. The complete amino acid sequences were determined from the sequences of tryptic peptides and CNBr cleaved fragments. Peptides were aligned by homology. The sequences of the two parvalbumins differed from each other in 22 residues but no variation was found in the residues that are responsible for calcium binding.
Two parvalbumins from the muscle of the electric eel, Electrophorus electricus, were purified by Sephadex G-50 gel filtration followed by DE-52 ion exchange column chromatography. From 350 g fresh eel muscle, 100-150 mg of pure major component (Parvalbumin I, = 4.25) can be isolated. The content of Parvalbumin II is around one-fifth of the major one, and its pI is 3.85. The complete amino acid sequences were determined from the sequences of tryptic peptides and CNBr cleaved fragments. Peptides were aligned by homology. The sequences of the two parvalbumins differed from each other in 22 residues but no variation was found in the residues that are responsible for calcium binding.