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16 results on '"McNally, Sheila F."'

8. Cytosolic glutamine synthetase in higher plants.

Author

Hirel, Bertrand, McNally, Sheila F., Gadal, Pierre, Sumar, Nazira, and Stewart, George R.

Subjects
*GLUTAMINE synthetase, *PLANT species, *IMMUNOGLOBULINS, *LIGASES, *BIOCHEMISTRY, *BIOMOLECULES, *ORGANIC compounds
Abstract

Cytosolic glutamine synthetase (GS1) was purified to homogeneity from etiolated barley leaves by DEAE-Sephacci and hydroxyapatite chromatography, gel filtration and polyacrylamide get electrophoresis. Specific antibodies against the purified protein were raised by the immunization of rabbits. Immunoprecipitation experiments demonstrated that cytosolic glut a mine synthetases isolated from the leaves of different plant species were very similar proteins. Good recognition of other cytosolic glutamine synthetases from roots, root nodular tissue and seeds by barley GS1 antibodies was obtained, suggesting that they too are all quite similar proteins In contrast, chloroplast glut amine synthetase (GS2) was considered to be a different protein in view of its low level of recognition by barley GS1 antibodies. [ABSTRACT FROM AUTHOR]

Published
1984
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9. Effects of phosphinothricin on the isoenzymes of glutamine synthetase isolated from plant species which exhibit varying degrees of susceptibility to the herbicide

Author

Ridley, Stuart M. and McNally, Sheila F.

Abstract

The herbicidal antibiotic phosphinothricin is a potent inhibitor of glutamine synthetase (EC 6.3.1.2) activity. There is considerable variation (almost 70-fold) in susceptibility towards phosphinothricin among a range of plant species. These plants show widely differing ratios of two isoenzymes of glutamine synthetase, but this does not correlate with whole-plant susceptibility to the herbicide. Analyses of the inhibition kinetics on the enzyme isolated from the same series of plants reveal similar Ki-values for phosphinothricin. The results indicate that the variation in whole-plant susceptibility to the herbicide is not caused by differences in the degree to which the glutamine synthetases from these plants are inhibited.

Published
1985
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10. Occurrence of Isóenzymes of Glutamine Synthetase in the Alga Chlorella kessleri1

Author

Sumar, Nazira, Casselton, Peter J., McNally, Sheila F., and Stewart, George R.

Subjects
Articles
Abstract

Two forms (GS(1) and GS(2)) of glutamine synthetase have been isolated, separated by ion exchange chromatography, and partly characterized from cells of the green alga Chlorella kessleri. Both forms are present in cells grown autotrophically or heterotrophically on various nitrogen sources, but under all nutritional conditions GS(1) was found to be the major isoenzyme present (60-80%). The activity of both isoenzymes was greatest in cells grown under nitrogen-limiting conditions. Both isoenzymes have molecular weights in the range 340 to 350,000 daltons. GS(1) was found to have a greater thermostability than GS(2): GS(1) was stable at 30 degrees C while GS(2) lost 95% of its activity in 30 minutes. GS(1) was much less sensitive to thiol reactive reagents than GS(2).

Published
1984

16. Symbiosis/The Biology of Symbiosis (Book).

Author

McNally, Sheila F.

Subjects
SYMBIOSIS (Book), BIOLOGY of Symbiosis, The (Book), AHMADJIAN, V., PARACER, S.
Abstract

Reviews the books 'Symbiosis. An Introduction to Biological Associations,' by V. Ahmadjian and S. Paracer and 'The Biology of Symbiosis,' by D.C. Smith and A.E. Douglas.

Published
1987
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