Isolation and characterization of the ram spermatidal nuclear proteins P1, 3 and T.
Ram spermatidal proteins P1, 3 and T were isolated from non-round spermatid nuclei and characterized by amino acid analysis. Spermatidal proteins are small arginine- and cysteine-rich basic proteins. Proteins P1 and T are unusually rich in serine and the histidine content of P1 is particularly high. The NaCl molarities required to dissociate these proteins from the spermatid nuclei were determined. These proteins are present only during the reorganization of the spermatid chromatin.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001120:Arginine / Q000032:analysis; D002467:Cell Nucleus / Q000032:analysis; D003545:Cysteine / Q000032:analysis; D004247:DNA / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D006639:Histidine / Q000032:analysis; D008297:Male; D009698:Nucleoproteins / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D010750:Phosphoproteins / Q000032:analysis; D010766:Phosphorylation; D012694:Serine / Q000032:analysis; D012756:Sheep; D012965:Sodium Chloride; D013087:Spermatids / Q000032:analysis* / Q000648:ultrastructure
D000596:Amino Acids; D006609:High Mobility Group Proteins; D009698:Nucleoproteins; D010750:Phosphoproteins; D012965:Sodium Chloride; D012694:Serine; D006639:Histidine; D004247:DNA; D001120:Arginine; D003545:Cysteine