Ad. Mcclung et al., IDENTIFICATION AND CHARACTERIZATION OF ATPASE ACTIVITY ASSOCIATED WITH MAIZE (ZEA-MAYS) ANNEXINS, Biochemical journal, 303, 1994, pp. 709-712
An ATPase activity is associated with maize (Zea mays) annexins. It ha
s a pH optimum of 6.0, shows Michaelis-Menten kinetics and is not stim
ulated by Ca2+, Mg2+, EDTA or KCl; it is not inhibited by vanadate, mo
lybdate, nitrate or azide, but N-ethylmaleimide inhibits by similar to
30% at 1-2 mM. These properties indicate that the activity is unlike
other ATPases, although it has many features in common with the myosin
ATPase. Gel filtration shows that the ATPase activity is mainly assoc
iated with a 68 kDa protein that is extracted with the p33/p35 annexin
s and cross-reacts with antibodies to these proteins.