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111.
Abscisic acid and water transport in sunflowers 总被引:5,自引:0,他引:5
The role of abscisic acid (ABA) in the transport of water and ions from the root to the shoot of sunflower plants (Helianthus annuus) was investigated by application of ABA either to the root medium or to the apical bud. The exudation at the hypocotyl stump of decapitated seedlings was measured with and without hydrostatic pressure (0–0.3 MPa) applied to the root. All ABA concentrations tested (10-10–10-4 mol·l-1) promoted exudation. Maximal amounts of exudate (200% of control) were obtained with ABA at 10-6·mol·l-1 and an externally applied pressure of 0.1 MPa. The effect was rapid and long-lasting, and involved promotion of ion release to the xylem (during the first hours) as well as an increase in hydraulic conductivity. Abscisic acid applied to the apical bud had effects similar to those of the rootapplied hormone. Increased rates of exudation were also obtained after osmotic stress was applied to the root; this treatment increased the endogenous level of ABA in the root as well as in the shoot. Water potentials of the hypocotyls of intact plants increased when the roots were treated with ABA at 5°C, whereas stomatal resistances were lowered. The results are consistent with the view that ABA controls the water status of the plant not only by regulating stomatal transpiration, but also by regulating the hydraulic conductivity of the root.Abbreviations and symbols ABA
abscisic acid
- Tv
volume flow
- Lp
hydraulic conductivity
- PEG
polyethyleneglycol
-
water potential
-
osmotic potential
-
osmotic value
- P
hydrostatic pressure 相似文献
112.
Neurotransmitter receptors and ion channels play a critical role in the transduction of signals at chemical synapses. The modulation of neurotransmitter receptor and ion channel function by protein phosphorylation is one of the major regulatory mechanisms in the control of synaptic transmission. The nicotinic acetylcholine receptor (nAcChR) has provided an excellent model system in which to study the modulation of neurotransmitter receptors and ion channels by protein phosphorylation since the structure and function of this receptor have been so extensively characterized. In this article, the structure of the nAcChR from the electric organ of electric fish, skeletal muscle, and the central and peripheral nervous system will be briefly reviewed. Emphasis will be placed on the regulation of the phosphorylation of nAcChR by second messengers and by neurotransmitters and hormones. In addition, recent studies on the functional modulation of nicotinic receptors by protein phosphorylation will be reviewed. 相似文献
113.
P Mentré F Escaig 《Biology of the cell / under the auspices of the European Cell Biology Organization》1992,74(1):119-126
Flotation on hot water (about 60 degrees C) which is frequently employed to stretch semithin sections on substrates for SIMS (secondary ion mass spectrometry) microscopy, is the cause of numerous artefacts. In the case of epoxy resin-embedded tissue, one observes loss of potassium and sodium and accumulation of calcium. The relative contrast of cell nuclei in the ionic images, is rapidly affected by these ion migrations. After prolonged contact with hot water, tissue becomes uniformly emissive. In the case of hydrosoluble resin-embedded tissue, potassium and sodium do not appear to be affected by the action of water, which suggests that they are covalently bound with chelating sites buried beneath the layer of water bound to the surface of the macromolecules. Calcium accumulates, probably on widely exposed anionic sites. Moreover, the domains observed in hydrosoluble resin-embedded tissue shrink differently according to the proportion of water removed by melamine; this can provide interesting information on the initial equilibrium between water, ion sand macromolecules. Our results seem to support the assumption that bound water should play an important role in the preservation of both macromolecular architecture and ion distributions. 相似文献
114.
115.
Summary In a survey of sperm antigens in the rat, a new intra-acrosomal antigen was found using a monoclonal antibody MC41 raised against rat epididymal spermatozoa. The MC41 was immunoglobulin G1 and recognized spermatozoa from rat, mouse and hamster. Indirect immunofluorescence with MC41 specifically stained the crescent region of the anterior acrosome of the sperm head. Immuno-gold electron microscopy demonstrated that the antigen was localized within the acrosomal matrix. Immunoblot study showed that MC41 recognized a band of approximately 165000 dalton in the extract of rat sperm from the cauda epididymidis. Immunohistochemistry with MC41 demonstrated that the antigen was first detected in approximately step-2 spermatids, and distributed over the entire cytoplasmic region of spermatids from step 2 to early step 19. The head region became strongly stained in late step-19 spermatids and then in mature spermatozoa. Distinct immunostaining was not found in the developing acrosome of spermatids throughout spermiogenesis. These results suggest that the MC41 antigen is a unique intra-acrosomal antigen which is accumulated into the acrosome during the terminal step of spermiogenesis. 相似文献
116.
H. H. Boer Cora Montagne-Wajer J. van Minnen Marja Ramkema Pamela de Boer 《Cell and tissue research》1992,268(3):559-566
Summary The functional morphology of the neuroendocrine system producing sodium influx-stimulating (SIS) peptide in the pond snail, Lymnaea stagnalis, was studied by in situ hybridization and immunocytochemistry. The SIS-peptide, which is 76 amino acids long, stimulates sodium uptake from the ambient medium. Two synthetic DNA probes were used for in situ hybridization. The nucleotide sequences were chosen from the cDNA structure; they encode amino acids 8–17 and 64–73, respectively. SIS-peptide sequences 10–20 and 67–76 were synthesized and antibodies were raised to them and affinity-purified. In addition to these antibodies, a monoclonal antibody raised to a bioactive, high-pressure liquid chromatography (HPLC)-purified brain extract was used for immunocytochemistry. Paraffin sections of central nervous systems and of whole snails were studied. The SIS-peptide system could be identified as the previously described yellow cell (YC) system by comparing alternate sections treated with the DNA probes, stained with the antibodies, or stained with alcian blue-alcian yellow. SIS-peptide neurons (45) occur in the ganglia of the visceral ring and in the proximal parts of visceral nerves. Axons run in the nerves of these and in several nerves of other ganglia. Numerous axon branches penetrate the perineurium forming a vast central neurohemal area. The SIS-peptide system innervates the pericardium, the nephridial gland, the reno-pericardial canal, the ureter, the spermoviduct and gonadal acini, the anterior aorta, the ventral buccal artery, and the penis protractor muscle. The morphology of the system is discussed in relation to the process of sodium ion uptake from the ambient medium and from pro-urine, and to that of regulating blood pressure. In the central nervous system and other organs, neurons and axons not labeled with the DNA probes, but immunoreactive to one or two of the antibodies, were observed. It seems unlikely that these elements are functionally related to the SIS-peptide system. 相似文献
117.
The protonmotive force in several sulfate-reducing bacteria has been determined by means of radiolabelled membrane-permeant probes (tetraphenyl-phosphonium cation, TPP+, for , and benzoate for pH). In six of ten freshwater strains tested only the pH gradient could be determine, while the membrane potential was not accessible due to nonspecific binding of TPP+. The protonmotive force of the other four strains was between –110 and –155 mV, composed of a membrane potential of –80 to –140 mV and a pH gradient between 0.25 and 0.8 (inside alkaline) at pHout=7. In Desulfobulbus propionicus the pH gradient decreased with rising external pH values. This decrease, however, was compensated by an increasing membrane potential. Sulfate, which can be highly accumulated by the cells, did not affect the protonmotive force, if added in concentrations of up to 4 mM. The highest sulfate accumulation observed (2500-fold), which occurred at external sulfate concentrations below 5 M, could be explained by a symport of three protons per sulfate, if equilibrium with the protonmotive force was assumed. At higher sulfate concentrations the accumulation decreased and suggested an electroneutral symport of two protons per sulfate. At sulfate concentrations above 500 M, the cells stopped sulfate uptake before reaching an equilibrium with the protonmotive force.Abbreviations CCCP
carbonyl cyanide m-chlorophenylhydrazone
- MOPS
morpholinopropanesulfonic acid
- TPP+
tetraphenylphosphonium cation
- EDTA
ethylenediaminetetraacetic acid
- pH
transmembrane pH gradient (pHin-pHout)
-
transmembrane electrical potential difference 相似文献
118.
The distribution of the F420-reactive and F420-nonreactive hydrogenases from the methylotrophic Methanosarcina strain Gö1 indicated a membrane association of the F420-nonreactive enzyme. The membrane-bound F420-nonreactive hydrogenase was purified 42-fold to electrophoretic homogeneity with a yield of 26.7%. The enzyme had a specific activity of 359 mol H2 oxidized · min-1 · mg protein-1. The purification procedure involved dispersion of the membrane fraction with the detergent Chaps followed by anion exchange, hydrophobic and hydroxylapatite chromatography. The aerobically prepared enzyme had to be reactivated anaerobically. Maximal activity was observed at 80°C. The molecular mass as determined by native gel electrophoresis and gel filtration was 77000 and 79000, respectively. SDS gel electrophoresis revealed two polypeptides with molecular masses of 60000 and 40000 indicating a 1:1 stoichiometry. The purified enzyme contained 13.3 mol S2-, 15.1 mol Fe and 0.8 mol Ni/mol enzyme. Flavins were not detected. The amino acid sequence of the N-termini of the subunits showed a higher degree of homology to cubacterial uptake-hydrogenases than to F420-dependent hydrogenases from other methanogenic bacteria. The physiological function of the F420-nonreactive hydrogenase from Methanosarcina strain Gö1 is discussed.Abbreviations
transmembrane electrochemical gradient of H-
- CoM-SH
2-mercaptoethanesulfonate
- F420
(N-l-lactyl--l-glutamyl)-l-glutamic acid phospodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin-5-phosphate
- F420H2
reduced F420
- HTP-SH
7-mercaptoheptanoylthreonine phosphate
-
Mb.
Methanobacterium
- PMSF
phenylmethyl-sulfonylfluoride
- Cl3AcOH
trichloroacetic acid 相似文献
119.
Tjakko Abee Jan Knol Klaas J. Hellingwerf Evert P. Bakker Annette Siebers Wil N. Konings 《Archives of microbiology》1992,158(5):374-380
Cells of the purple non-sulphur bacterium Rhodobacter sphaeroides express a high-affinity K+ uptake system when grown in media with low K+ concentrations. Antibodies againts the catalytic KdpB protein or the whole KdpABC complex of Escherichia coli crossreact with a 70.0 kDa R. sphaeroides protein that was expressed only in cells grown in media with low K+ concentrations. In membranes derived from R. sphaeroides cells grown with low K+ concentrations (induced cells), a high ATPase activity could be detected when assayed in Tris-HCl pH 8.0 containing 1 mM MgSO4. This ATPase activity increased upon addition of 1 mM KCl from 166 to 289 mol ATP hydrolysed x min-1 x g protein-1 (1.7-fold stimulation). The K+-stimulated ATPase activity was inhibited approximately 93% by 0.5 mM vanadate but hardly by N,N-dicyclohexylcarbo-diimide (DCCD). These results indicate that the inducible K+-ATPase in R. sphaeroides resembles the Kdp K+-translocating ATPase of Escherichia coli. This Kdp-like transport system is also expressed in R. capsulatus and Rhodospirillum rubrum during growth in media with low K+ concentrations suggesting a wide distribution of this transport system among phototrophic bacteria.Abbreviations
electrical potential difference across the cytoplasmic membrane
- pH
pH difference across the cytoplasmic membrane
- BSA
bovine serum albumine
- PAGE
polyacrylamide gel electrophoresis
- HEPES
4-(2-hydroxyethyl)-1-piperazine-ethanesulfonic acid
- PMSF
phenyl-methyl-sulfonyl fluoride
- DCCD
N,N-dicyclohexylcarbodiimide
- AIB
2--aminoisobutyric acid
- TMG
methyl--d-thiogalactopyranoside 相似文献
120.
The hemolymph of the adult female Manduca sexta was fractionated by cascade-mode multi-affinity chromatography (CASMAC) on a main-line tandem column chain containing Zn(2+)-TED, T-gel, Ni(2+)-DPA, and phenylsepharose and a side-line column containing Zn(2+)-DPA. The technique separated some of the previously described major hemolymph proteins, and yielded a number of fractions with simple composition. Some of these fractions contained only less abundant proteins of Manduca hemolymph. Thus, it appears that CASMAC would be a very useful fractionation technique for purification and characterization of the minor proteins of insect hemolymph. 相似文献