Protein Storing Vacuoles in Ray Ceils of Willow Wood (Salix Caprea L.)

IAWA Journal ◽  
1988 ◽  
Vol 9 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Jörg J. Sauter ◽  
Silvia Wellenkamp

Light- and electron-microscopical investigations revealed protein bodies of c. 0.5 to 2.5 µm in diameter in the ray cells of willow wood. They consist of electron-dense aggregatesofvarious structural organisation which are enclosed in small-sized vacuole-like compartrnents. In semi-thin sections these aggregates showed positive protein staining with Ponçeau Red and Coomassie Blue, and enzymatic digestibility with pepsin. Because these protein bodies are found during the dormant season but not during summer, they are believed to be specific sites of protein storage in the ray cells of the wood. This is in accordance with the biochemical protein determination which yielded 6.4 to 8.4 µg mg-1 dry weight in late fall but only 1.2 to 2.0 µg mg-1 dry weight during summer.

Author(s):  
S. Lehner ◽  
H.E. Bauer ◽  
R. Wurster ◽  
H. Seiler

In order to compare different microanalytical techniques commercially available cation exchange membrane SC-1 (Stantech Inc, Palo Alto), was loaded with biologically relevant elements as Na, Mg, K, and Ca, respectively, each to its highest possible concentration, given by the number concentration of exchangeable binding sites (4 % wt. for Ca). Washing in distilled water, dehydration through a graded series of ethanol, infiltration and embedding in Spurr’s low viscosity epoxy resin was followed by thin sectioning. The thin sections (thickness of about 50 nm) were prepared on carbon foils and mounted on electron microscopical finder grids.The samples were analyzed with electron microprobe JXA 50A with transmitted electron device, EDX system TN 5400, and on line operating image processing system SEM-IPS, energy filtering electron microscope CEM 902 with EELS/ESI and Auger spectrometer 545 Perkin Elmer.With EDX, a beam current of some 10-10 A and a beam diameter of about 10 nm, a minimum-detectable mass of 10-20 g Ca seems within reach.


Author(s):  
Hsin-Kan Wu ◽  
Mei-Chu Chung

In one of our earlier papers (Wu et al. 1978), we suggested that glutelin is the major composition of the round storage protein bodies although they also contain relatively more prolamine than the angular one does. Immunochemical studies of Krishnan et al. (1986) later showed the presence of glutelin in the irregularly-shaped (angular) protein bodies while the prolamines were found in the round ones. Our recent experiment using protein A-gold technique found that prolamine is mainly deposited into the angular protein bodies.Small blocks (1 mm3) of 7 DAF (days after flowering) caryopsis of Orvza perennis were fixed with 3% paraformaldehyde and 3% glutaraldehyde in 0.1M sodium phosphate, pH7.4, dehydrated in a graded ethanol series and infiltrated with Spurr’s resin. Thin sections, after gold labeling, were stained with uranyl acetate and lead citrate. Rabbit antibodies were raised against purified prolamine. Protein A-gold sol complex was prepared based on the technique of Horisberger et al. (1977).


1975 ◽  
Vol 55 (1) ◽  
pp. 185-190 ◽  
Author(s):  
S. PANDEY ◽  
E. T. GRITTON

Nine cultivars of peas (Pisum sativum L.) were grown in 1971 and 1972 to study the changes in percent crude protein levels during maturation. Percent protein was found to vary with years, cultivars, and stages of maturity. The year × cultivar, year × maturity, and cultivar × maturity interactions were also important. On a dry weight basis, pea protein concentration as determined by the Kjeldahl method showed a decrease with increasing pea seed maturity through the canning stage. The correlation coefficient between the Kjeldahl and Udy dye-binding methods of protein determination was 0.86 at the mature seed stage, and negligible at the canning stage. There was a highly significant correlation (r = 0.91) between protein concentration at the canning and mature stages of seeds (Kjeldahl method). The correlation coefficient between protein values obtained by the dye-binding method of Ashworth et al. and the Kjeldahl method was lower than between the Kjeldahl and Udy methods.


1980 ◽  
Vol 28 (1) ◽  
pp. 1 ◽  
Author(s):  
PJ Hocking ◽  
J Kuo ◽  
JS Pate

The mineral nutrition of developing fruits of the hemiparasite Nuytsia floribunda was studied in natural habitat near Perth, W.A. Nuytsia fruits were similar to those of other higher plants in their mineral nutrition. Changes in the contents of specific nutrients in fruits and their bracts were described. Accumulation of mineral elements in fruits and bracts was synchronized closely with the acquisition of dry matter. Bracts lost 45-75% of their nitrogen, phosphorus, sulfur, zinc and copper, 16-29% of their potassium, magnesium, iron and manganese, but less than 5% of their calcium and sodium during senescence. Mobilization from bracts was estimated to provide 0-35% of the fruit's accumulation of specific nutrients. Analysis of xylem sap showed that asparagine was the main solute for transport of nitrogen. Mature seedsconsisted mainly of a thick layer of endosperm surrounding the embryo and cotyledons. Seeds contained 31% oil, 35% protein, but no storage carbohydrate. Scanning X-ray microprobe analysis on thin sections of endosperm showed that phosphorus, sulfur, calcium, magnesium and iron were associated with protein bodies. Manganese was localized in certain iron-rich protein bodies.


IAWA Journal ◽  
1989 ◽  
Vol 10 (4) ◽  
pp. 395-403 ◽  
Author(s):  
Jörg J. Sauter ◽  
Barbara van Cleve

The size and distribution of individual cell organelles (plastids, mitochondria, oleosomes, protein bodies) and of the three main storage compounds (starch, fat, protein) have been studied micromorphometrically at the electron microscopical level in ray cells of poplar wood during early winter. The three cell types of the rays (contact cells, isolation cells, cells of the contact cell rows) show remarkable differences in size and distribution of organelles and of storage material which manifest an existing physiological specialisation of these cells. The micromorphometric data on storage compounds are compared with the biochemically determined amounts of starch, proteins, fat-bound glycerol, and of various sugars in the wood. At the stage investigated, a prominent protein storage, an extensive starch-sugar transition, but no indications for a starch-fat transition are found. Micromorphometry proved to be a useful tool for the detection of cell-specific differences within a tissue.


1992 ◽  
Vol 3 (5) ◽  
pp. 319-322 ◽  
Author(s):  
Ralph L. Amateis ◽  
Harold E. Burkhart ◽  
Phillip H. Dunham

Author(s):  
Paweł Piotr Pieta ◽  
Ewa Burchacka ◽  
Aleksandra Śliwa ◽  
Anna Szczerba

Polyacrylamide gel electrophoresis, followed by an appropriate staining, is a popular and useful analytical procedure for protein identification and characterization. The aim of this study was to develop a method for protein visualization in polyacrylamide gels that would be alternative to Coomassie blue or silver staining. The proposed method is simple, fast and inexpensive. The optimized protocol for protein staining and visualization takes as little as 6 minutes and utilizes deionized water and chloroform. Fluorescence of proteins is induced by UV light and can be detected with a standard transilluminator.


Author(s):  
K. Kuroda ◽  
A. H. Heuer

Lead zirconate titenate (Pb(Zr,Ti)O3, PZT) is a well known piezoelectric substance. Three phases have been reported in modified PbZr0.95Ti0.05O3 (PZT 95/5) bodies -- a low temperature rhombohedral ferroelectric phase (FR1), a high temperature rhombohedral ferroelectric phase (FR2) and a cubic paraelectric phase (PC). A pressure induced ferroelectric to antiferroelectric phase transformation has also been reported in modified PZT 95/5 ceramics. These phase transformations are of technological importance, as this ceramic has practical applications as a power source in which large quantities of charge are released by shock wave depolarization.Both as-fired and pressure de-poled samples of PZT 95/5 ceramics with 0.8% Nb were investigated by transmission electron microscopy. Specimens for electron microscopical study were prepared from thin sections, which had been sliced by diamond saw and then mechanically polished with 600 grit SiC paper followed by diamond polishing to about 100 μm thickness. These specimens were then argon ion milled to electron transparency; a liquid N2 cooled stage was used to try and prevent the occurrence of phase transformations due to heating during ion beam thinning. Special care was also taken to minimize beam heating during electron microscopical observation.


1978 ◽  
Vol 56 (17) ◽  
pp. 2050-2061 ◽  
Author(s):  
John N. A. Lott ◽  
Mark S. Buttrose

Protein bodies from almond (Prunus dulcis), Brazil nut (Bertholletia excelsa), and quandong (Santalum acuminatum) have been studied in thin sections of fixed and embedded tissue, in freeze-fracture replicas of unfixed tissue, by chemical analysis of tissue for P, K, Mg, and Ca, and by energy dispersive x-ray (EDX) analysis of both sections of glutaraldehyde-fixed tissue and freeze-dried tissue powders. The protein bodies in all three species contained globoid crystals, protein crystalloids, and proteinaceous matrix regions. Results of EDX analyses were consistent with globoid crystals being rich in phytin. Variation in both the structure and the elemental composition of globoids was common. In almond some globoids were lobed rather than spherical, and large globoid crystals often contained considerable calcium whereas small globoid crystals contained little if any calcium. The globoid crystals of Brazil nut often contained barium in addition to P, K, Ca, and Mg. Protein crystalloids of Brazil nut were compound crystals. Protein bodies of quandong seed, which is largely endosperm rather than embryo, were unexceptional.


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