Identification and characterization of ATPase activity associated with maize (Zea mays) annexins.

摘要: An ATPase activity is associated with maize (Zea mays) annexins. It has a pH optimum of 6.0, shows Michaelis-Menten kinetics and not stimulated by Ca2+, Mg2+, EDTA or KCl; it inhibited vanadate, molybdate, nitrate azide, but N-ethylmaleimide inhibits approximately 30% at 1-2 mM. These properties indicate that the unlike other ATPases, although many features in common myosin ATPase. Gel filtration mainly 68 kDa protein extracted p33/p35 annexins cross-reacts antibodies to these proteins.