title: Properties of kinesin isolated from human prostatic DU 145 tumor cells and bovine brain.
abstract: We have isolated and compared the 116-kilodalton (kDa) kinesin heavy chain from DU 145 human prostatic tumor cells and bovine brain. Comparative sodium dodecyl sulfate - polyacrylamide gel electrophoreses (SDS-PAGE), Western blots, and proteolytic digestion analysis all showed that the 116-kDa polypeptides from both sources were indistinguishable. Polyclonal antibodies raised against sea urchin kinesin cross-reacted with both brain and DU 145 kinesin on Western blots. SDS-PAGE and A-5m chromatographic studies indicated that kinesin forms a quarternary heteropolymer of approximately 400 kDa. DU 145 cells had three proteins of 116, 72, and 64 kDa forming the heteropolymer, in a 2:1:1 ratio, whereas brain cells appeared to have equimolar amounts of the 116-kDa heavy chain and a 64-kDa light chain.
authors: Department of Pharmacology, Fox Chase Cancer Center, Philadelphia, PA 19111.
authors: M E
authors: ME
authors: Stearns
authors: G A
authors: GA
authors: Piazza
mesh_terms: D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D016547:Kinesins; D008297:Male; D008868:Microtubule Proteins / Q000302:isolation & purification; D008970:Molecular Weight; D011471:Prostatic Neoplasms / Q000032:analysis; D014407:Tumor Cells, Cultured / Q000032:analysis*
chemical_list: D008868:Microtubule Proteins; D000251:Adenosine Triphosphatases; D016547:Kinesins