Sequence and characterization of the sperm-specific protein phi 3 from Mytilus californianus.
We have shown that the sperm-specific protein phi 3 from Mytilus californianus (Conrad) exhibits compositional microheterogeneity. For the first time, we have isolated and characterized the three major components of this protein. These fractions display different electrophoretic mobilities on Triton/urea/acetic acid polycrylamide gels. However, they have a very similar molecular mass of 5 +/- 0.1 kDa as measured by sedimentation equilibrium in the analytical ultracentrifuge. All of them show a marked trend toward aggregation. We have also established the sequence for each of these three fractions. The sequencing data suggest an even greater extent of microheterogeneity for this protein. The predicted secondary structure from the sequences, as well as infrared analyzes carried out on the native protein, suggest a structure organization into an alpha helix.
Ausio
J
J
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331.
McParland
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D049872:Bivalvia / Q000378:metabolism*; D005591:Chemical Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D011487:Protein Conformation; D011506:Proteins / Q000302:isolation & purification*; D014461:Ultracentrifugation
D009687:Nuclear Proteins; D010446:Peptide Fragments; D011506:Proteins; C026588:sperm basic nuclear proteins; C060562:sperm-specific protein phi3; D010447:Peptide Hydrolases