Detail of "9067-77-0"

Reference

Regulation of levels of nuclear transcripts for C4 photosynthesis in bundle sheath and mesophyll cells of maize leaves

Regulation of levels of nuclear transcripts for C4 photosynthesis in bundle sheath and mesophyll cells of maize leaves. Sheen, Jenq Yunn; Bogorad, Lawrence (Dep. Cellular Dep. Biol., Harvard Univ., Cambridge, MA 02138, USA). Plant Mol. Biol., 8(3), 227-38 (English) 1987.Several reagents with their cas registry numbers 9027-23-0 and 9001-52-9 are used here. CODEN: PMBIDB. ISSN: 0167-4412. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Genetics) Section cross-reference(s): 6, 11 In vitro translation of polyA+ mRNAs isolated from purified maize bundle sheath and mesophyll cells results in the prodn. of distinctive cell-specific polypeptides. Immunopptn. expts. show that translatable polyA+ mRNAs for phosphoenolpyruvate carboxylase (PEPC) [9067-77-0], pyruvate orthophosphate dikinase (PPDK) [9027-40-1], and NADP-malate dehydrogenase [37250-19-4] are prominent in mesophyll but not bundle sheath cells. On the contrary, those for sedoheptulose-1,7-bisphosphatase [9055-32-7], fructose-1,6-bisphosphatase [9001-52-9], NADP-malic enzyme (ME) [9028-47-1], and the small subunit of ribulose-1,5-bisphosphate carboxylase (RuBPCSS) [9027-23-0] are present only in bundle sheath cells. Moreover, polyA+ mRNA is encoding the 33-kD, 23-kD, and 16-kD polypeptides of the oxygen-evolving complex (OE33, OE23, and OE16) and the light-harvesting chlorophyll a/b-binding protein of photosystem II (LHCP II) are much more abundant in mesophyll than in bundle sheath cells. Northern blot analyses with cDNA clones of PEPC, PPDK, ME, RuBPC, SS, OE33, OE23, OE16, and LHCP II are consistent with the conclusion that the cell-specific expression of these genes is regulated at the RNA level. The RNA level differences are esp. dramatic in dark-grown maize seedlings after illumination for 24 h. .

An investigation into the influence of IAA and malate on in vivo and in vitro rates of dark carbon dioxide fixation in coleoptile tissue

An investigation into the influence of IAA and malate on in vivo and in vitro rates of dark carbon dioxide fixation in coleoptile tissue. Dymock, I. J.; Hill, B.; Bown, A. W. (Dep. Biol. Sci., Brock Univ., St. Catharines, Ont., Can.). Can. J. Bot., 55(12), 1641-5 (English) 1977. CODEN: CJBOAW. DOCUMENT TYPE: Journal CA Section: 5 (Agrochemicals) Etiolated Avena sativa cv. Victory coleoptiles were used to det. the influence of indole-3-acetic acid (I) [87-51-4] or malate [6915-15-7] on in vivo and in vitro rates of CO2 [124-38-9] fixation. In addn., the influence of malate on IAA-stimulted growth was investigated. Concns. of malate which stimulate growth did not influence the in vivo rate of dark [14C]bicarbonate fixation but did inhibit in vitro phosphoenolpyruvate carboxylase (EC 4.1.1.31) [9067-77-0] activity. IAA did not influence this enzymic activity or reduce the inhibition of the enzyme by malate, and the rate of [14C]bicarbonate fixation was not measurably influenced by 20 .mu.M IAA within the time period required for IAA stimulation of growth to become apparent. In the absence of atm. levels of CO2, 1 mM malate and 20.mu.M IAA stimulate growth in a weakly synergistic manner. These results are discussed in relation to a suggestion that IAA-stimulated H+ secretion and growth involves a rapid effect on CO2 fixation.