Abstract
The protamines from the emitted sperm nuclei of the marine annelid Platynereis dumerilii have been purified from the whole basic protein by gel filtration and ion-exchange chromatography and further fractionated by reverse-phase high-performance liquid chromatography. Four main fractions were obtained and characterized by their electrophoretic mobilities and amino acid compositions. All these protamines are characterized by high arginine and serine contents and by the presence of equivalent amounts of asparagine, threonine and valine. Each of these fractions is heterogeneous. After re-fractionation the amino acid composition and the N-terminal sequence of the samples indicate that each protein corresponds to a variant of the same family of highly related protamines.
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