Pea roots

Bewley, J.D. Larsen, K. (1980). Cessation of protein synthesis in water-stressed pea roots and maize mesocotyls without loss of polyribosomes. Effects of lethal and non-lethal water stress. Journal of Experimental Botany, 32, 1245-56. 

L. Sk0t and H. Egsgaard, Identification of ononitol and O-methyl-scyllo-inositol in pea root nodules. Plania 161 32-36 (1984). 

Yang, W.C. et al.. In situ localization of chalcone synthase mRNA in pea root nodule development, Plant J., 2, 143, 1992. 

A lithium chloride solution caused changes in gravicur-vature, statocyte ultrastructure, and calcium balance in pea root, believed to be due to effects of lithium on the phosphoinositide second messenger system (678). The implications with regard to human parathyroid function are obscure. 

Belyavskaya NA. Lithium-induced changes in gravicurva-ture, statocyte ultrastructure and calcium balance of pea roots. Adv Space Res 2001 27(5) 961-6. 

Benhamou, N., Kloepper, J.W., Quadt-Hallman, A., Tuzun, S. Induction of defence-related ultrastructural modifications in pea root tissues inoculated with endophytic bacteria. Plant Physiol 1996 112 919-929. 

Tu, J.C., Findlay, W.I. The effects of different green manure crops and tillage practices on pea root rots. British Crop Protection Conference - Pest and Diseases. British Crop Protection Council Publ. Surrey, U.K. 1986 pp. 229-236... 

Kannenberg, E.L., Perotto, S., Bianciotto, V. Rathbum, E.A., Brewin, N.J., lipopolysaccharide epitope expression of Rhizobium bacteroids as revealed by in situ immunolabelling of pea root nodule sections. J Bacteriol 176 (1994) 2021-2032. 

Perotto, S., VandenBosch, K.A., Butcher, G.W., Brewin, N.J. Molecular composition and development of the plant glycocalyx associated with the peribacteroid membrane of pea root nodules. Development 112 (1991) 763-773. 

Porath, E. and A. Poljakoff-Mayber. 1964. Effect of salinity on metabolic pathways in pea root tips. Isr. J. Bot. 13 115—121. 

In short, cell fractionation, which is composed of three steps—homogenization, fractionation, and analysis—can be an excellent way to locate an enzyme within the cell. The reader is referred to the excellent commentary by ap Rees (1995), in which the rigorous criteria to follow so that a cell fractionation provides good, reliable information is summarized. The author concludes that work done on soybean protoplasts (Macdonald and ap Rees, 1983), wheat endosperm protoplasts (Entwistle and ap Rees, 1988), wheat endosperm (Tetlow et al., 1993), pea embryos (Denyer and Smith, 1988), and pea roots (Borchert et al., 1993) provides further support for the view that ADPGlc PPase essentially is confined to the plastid. 

Borchert, S., Grosse, H., and Heldt, H. W. 1989. Specific transport of inorganic phosphate, glucose 6-phosphate, dihydroxyacetone phosphate and 3-phospho-glycerate into amy-loplasts from pea roots. Fed. Eur. Biochem. Soc. 253,183-186. 

Borchert, S., Harbroth, J, Schilnemann, D., Hoferichter, P., and Heldt, H. W. 1993. Studies of the enzymic capacities and transport properties of pea root plastids. Plant Physiol. 101, 303-312. 

The results of the only foundational experiments that explored the identity of a reaction sequence (mechanism) for the PPP were published by the Horecker group (40, 41). Detailed treatment of the conduct and conclusions of these important, but rarely discussed, experiments is given in References 1 and 42. A prediction labeling technique that used [1- C]- and [2,3- C]-Rib 5-P as substrates was adopted. These substrates were reacted with fractionated enzyme extracts of acetone powder preparations from rat liver, pea leaf, and pea root tissues and formed, among other intermediates, C -labeled Glc-6-P (Fig. 3) and glyceraldehyde 3-P (Gra 3-P) (41). It was anticipated that both the position and the amount of C-label imparted to the Glc 6-P formed by the above substrates would reveal the nature and order of the reactions involved in its formation. 

Gibbs M, Horecker BL. The mechanism of the conversion of pentose phosphate to hexose monophosphate II. With pea leaf and pea root preparations. J. Biol. Chem. 1954 208 813-820. 

Relatively few detailed studies have been performed on the GDH s of plants. An enzyme active with NAD but not NADP has been purified 1250-fold from pea roots (4S)- When assayed by reductive amination, however, the rate of reaction is 1.8 times faster with NADPH than NADH. An NAD-linked enzyme has been isolated from soybean cotyledons (47), and a similar enzyme from com leaves (4 ) has been shown not to be affected by purine nucleotides (17). 

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