Identification of microtubule-associated proteins in the meiotic spindle of surf clam oocytes.
Meiotic spindles isolated from surf clam oocytes to morphological purity are biochemically complex, consisting of many polypeptides. These proteins fall into two classes: (a) polypeptides that are apparently cytoplasmic proteins and are not specifically associated with the spindle; and (b) polypeptides that are specifically associated with the spindle. A subset of the spindle-associated proteins, including a 250,000 mol wt component, remain with spindle tubulin through cycles of cold depolymerization and warm polymerization, showing that they are microtubule-associated proteins.
D000818:Animals; D049872:Bivalvia; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005990:Glycerol; D006018:Glycols; D008540:Meiosis; D008870:Microtubules / Q000032:analysis*; D009698:Nucleoproteins / Q000032:analysis*; D009865:Oocytes / Q000648:ultrastructure*; D009940:Organoids / Q000648:ultrastructure*; D010063:Ovum / Q000648:ultrastructure*; D010455:Peptides / Q000032:analysis; D014404:Tubulin / Q000032:analysis*
D006018:Glycols; D009698:Nucleoproteins; D010455:Peptides; D014404:Tubulin; D005990:Glycerol