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The Biological Bulletin, Vol 182, Issue 1 31-40, Copyright © 1992 by Marine Biological Laboratory

DEVELOPMENT AND REPRODUCTION

Purification and Biochemical Characterization of the Nuclear Sperm-Specific Proteins of the Bivalve Mollusks Agriodesma saxicola1 and Mytilimeria nuttalli

J. Ausio
Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada

The proteins from the nuclei of the sperm from two different species of the subclass Anomalodesmata of the class Bivalvia have been analyzed for the first time. In both instances--Agriodesma saxicola (Baird, 1863) and Mytilimeria nuttalli (Conrad, 1837)--the compositional pattern is very similar. The sperm chromatin is organized by a major protamine-like PL-I protein. As in all PL-I, this protein has a trypsin-resistant core. In both species analyzed, PL-I contains cysteine residues that account for the presence of the monomer (M) and dimer (D) forms observed in the total nuclear HCl extracts. The molecular mass of these proteins is 21,000 Da in A. saxicola, and 25,000 Da in M. nuttalli. All of the specimens of A. saxicola analyzed were hermaphrodites. As a result, the nuclear sperm-specific proteins from several preparations were readily and extensively degraded by protease activity from the oocytes. Such degradation was always observed when cross contamination between the two gonadal tissues accidentally occurred during protein extraction.




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Copyright © 1992 by the Marine Biological Laboratory.