Abstract
The dynein β heavy chain and the intermediate chain 1 (IC1) from sea urchin sperm flagella cosediment at 11S through sucrose density gradient centrifugation. When the isolated β/IC1 complex was treated with a bifunctional cross-linker, dimethyl suberimidate (DMS), and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, four high molecular mass products appeared on the gel. Immunoblotting of the products with affinity-purified polyclonal antibodies against β heavy chain and IC1 revealed that these were cross-linked products of β heavy chain and IC1. Treatment of β/IC1 complex with DMS activated the ATP hydrolysis and decreased its sensitivity to inhibition by vanadate
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