Effects of AMPPNP and vanadate on the mechanochemical crossbridge cycle in flagella.
The non-hydrolysable ATP analogue, beta,gamma-imido-adenosine-5'-triphosphate (AMPPNP, adenylilimidodiphosphate) does not reduce the stiffness of demembranated sea urchin sperm flagella measured in the rigor state in the absence of MgATP2- and does not cause relaxation of rigor bends. The competitive inhibitions provide further evidence that the dynein-tubulin crossbridge cycle in flagella is similar to the actin-myosin crossbridge cycle.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology*; D000818:Animals; D004398:Dyneins / Q000378:metabolism; D008297:Male; D012617:Sea Urchins; D013082:Sperm Tail / Q000187:drug effects / Q000378:metabolism*; D013094:Spermatozoa / Q000378:metabolism*; D014404:Tubulin / Q000378:metabolism; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
D014404:Tubulin; D014639:Vanadium; D000266:Adenylyl Imidodiphosphate; D014638:Vanadates; D000255:Adenosine Triphosphate; D004398:Dyneins