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

Content Provider	Semantic Scholar
Author	McClung, A. D. Carroll, Andrew D. Battey, Nicholas H.
Copyright Year	1994
Abstract	An ATPase activity is associated with maize (Zea mays) annexins. It has a pH optimum of 6.0, shows Michaelis-Menten kinetics and is not stimulated by Ca2+, Mg2+, EDTA or KCl; it is not inhibited by vanadate, molybdate, nitrate or azide, but N-ethylmaleimide inhibits by approximately 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 associated with a 68 kDa protein that is extracted with the p33/p35 annexins and cross-reacts with antibodies to these proteins.
Starting Page	599
Ending Page	604
Page Count	6
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/303/3/709.full.pdf
PubMed reference number	7980436v1
Volume Number	303
Part	3
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Subject Keyword	Annexins Azides Edetic Acid Ethylmaleimide Extraction Nitrates Phase I/II Trial Potassium Chloride Vanadates corn extract corn pollen extract 50 MG/ML Injectable Solution molybdate
Content Type	Text
Resource Type	Article

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