M. Daban et al., SEQUENCE-ANALYSIS AND STRUCTURAL FEATURES OF THE LARGEST KNOWN PROTAMINE ISOLATED FROM THE SPERM OF THE ARCHAEOGASTROPOD MONODONTA-TURBINATA, Journal of molecular evolution, 40(6), 1995, pp. 663-670
Protamine of the archaeogastropod mollusc Monodonta turbinata has been
isolated and characterized. With a mass of 13,476 Da, it is the large
st known protamine. Amino acid sequence of this protamine (106 residue
s) was established from data provided by automated sequence analysis a
nd mass spectrometry of the protein and of its fragments. The primary
structure of the NH2-terminal region exhibits repetitive sequence moti
fs ''Basic-Ser'' (mainly R-S) and both central and COOH-terminal regio
ns are composed by arginine clusters. The amino acid sequence of Monod
onta turbinata protamine shows structural similarities with other prot
amines from invertebrates and from birds and mammals.