A basic protein has been isolated from sperm of the bivalve Spisula solidissima. Its characteristics are reminiscent of both histone H1 and of fish protamines. It is unusual in several respects: it contains similar amounts of lysine (24.8%) and arginine (23.1%), plus a residue of tryptophan per molecule. Its size is very large, approximately 297 amino acid residues. It shows a tendency to aggregate, an unusual property given the strongly charged nature of this protein.
No takes yet. Share an insight, caveat, or question.
Ausió et al. (1982) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: