NDLI: Adenosine triphosphatase from soybean callus and root cells.

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Adenosine triphosphatase from soybean callus and root cells.

Content Provider	Semantic Scholar
Author	Hendrix, Donald L. Kennedy, Robert M.
Copyright Year	1977
Abstract	The ATPase activity of a membrane fraction from soybean (Glycine max L.) root and callus cells, presumed to be enriched in plasma membrane, has been characterized with respect to ion stimulation, pH requirement, and nucleotide specificity. The enzyme from both sources was activated by divalent cations (Mg(2+) > Mn(2+) > Zn(2+) > Ca(2+) > Sr(2+)) and further stimulated by monovalent salts. Preparations from root cells were stimulated by monovalent ions according to the sequence: K(+) > Rb(+) > Choline(+) > Na(+) > Li(+) > NH(4) (+) > Cs(+) > tris(+). Membrane preparations from callus cells showed similar stimulatory patterns except for a slight preference for Na(+) over K(+). No synergism between K(+) and Na(+) was found with preparations from either cell source.The pH optimum for ATP hydrolysis in the presence of 50 mm KCl and 3 mm MgSO(4) was 6.5 for both preparations and slightly higher in the presence of 3 mm MgSO(4) alone. The order of nucleotide preference was found to be: ATP >> ADP > GTP > CTP > UTP. Maximal glucan synthetase activity at high (1 mm), but not at low (1 mum), substrate was found to be coincident with the position of this fraction on the sucrose gradient.
Starting Page	122
Ending Page	122
Page Count	1
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.plantphysiol.org/content/plantphysiol/59/2/264.full.pdf
PubMed reference number	16659830v1
Volume Number	59
Issue Number	2
Journal	Plant physiology
Language	English
Access Restriction	Open
Subject Keyword	1,3-beta-D-glucan synthase activity ATP Hydrolysis Adenosine Diphosphate Adenosine Triphosphate Bile Salts Bone callus Calcium Cations Cations, Divalent Glycine Guanosine Triphosphate Iontophoresis Nucleotides Plasma membrane Potassium Chloride Rubidium Soybeans Sucrose Tissue membrane Uridine Triphosphate ligase activity lithium cation micacocidin A
Content Type	Text
Resource Type	Article

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