000			02099cab a2200301Ia 45 0
001			u195506
003			SIRSI
008			111011s2005 ua ss b eng d
040			_aEAL
041			_aeng _bara
090			_aART AAR V10 No1 16
100	1		_aEl-Kassabany, Shafika A.
240	1	0	_aJournal of the advances in agricultural researches, 2005 v. 10 (1) _h[electronic resource].
245	1	0	_aSolubilization, purification, and characterization of the ATPase from spinach leaves plasma membrane fraction and its sensitivity to herbicides _h[electronic resource].
246	1	5	_aفصل وتنقية إنزيم الأدينوزين ثالث الفوسفاتيز من الغشاء السيتوبلازمى لخلايا أوراق السبانخ دراسة خصائصة وتاثير مبيدات الحشائش عليه.‪‪
300			_aP. 259-268.
504			_aIncludes references.
520			_aThe plasma membrane ATPase of spinach leaves (Spinacia oleracea) bad been solubilized with a two-step procedure using the anionic detergent, deoxycbolate (DOC) and the non ionic detergent, aminoxid WS35 as follows: I) loosely bound membrane proteins are removed by treatment with 0.1% DOC; 2) The ATPase is solubilized with 0.1 % aminoxid WS35 in the presence of 1 % DOC; 3) the solubilized material is further purified by centrifugation through a glycerol gradient (45-70%). Typically, about 10% of the ATPase activity is recovered, and the specific activity increases about II-fold. The properties of the purified ATPase are essentially the same as those of membrane-bound ATPase, with respect to substrate specificity, inhibitor sensitivity, and ion stimulation.
546			_aSummary in Arabic.
650		0	_aPlant cell walls.
650		0	_aSolubilization.
650		0	_aAdenosine triphosphatase.
650		0	_aHerbicides _xApplication.
650		0	_aSpinach _xComposition.
773	0		_tJournal of the Advances in Agricultural Researches. _g2005.v.10(1) _x1110-5585 _7nnas _wu158404
856	4	0	_uhttp://nile.enal.sci.eg/EALE/2005/AAR/1005/1/259.pdf _zFull Text Article
596			_a1
942			_cAR _2lcc
999			_c48647 _d48647