Electron Microscopy Related to the Reserve Mobilization in Germinating Rice Seed: —Decomposition process of protein bodies—

1999 ◽  
Vol 2 (2) ◽  
pp. 100-108 ◽  
Author(s):  
Sabaruddin Zakaria ◽  
Toshiaki Matsuda
Keyword(s):  
Electron Microscopy ◽  
Decomposition Process ◽  
Protein Bodies ◽  
Rice Seed ◽  
Reserve Mobilization

Deposition of a recombinant peptide in ER-derived protein bodies by retention with cysteine-rich prolamins in transgenic rice seed

Planta ◽  
2009 ◽  
Vol 229 (5) ◽  
pp. 1147-1158 ◽  
Author(s):  
Fumio Takaiwa ◽  
Sakiko Hirose ◽  
Hidenori Takagi ◽  
Lijun Yang ◽  
Yuhya Wakasa
Keyword(s):  
Transgenic Rice ◽  
Protein Bodies ◽  
Rice Seed ◽  
Recombinant Peptide ◽  
Transgenic Rice Seed

scholarly journals The influence of jasmonic acid on the amount and the distribution of cysteine proteinase PLCP-2 in healthy and PVYNTN infected potato plants (Solanum tuberosum L.)

2002 ◽  
Vol 38 (SI 1 - 6th Conf EFPP 2002) ◽  
pp. S95-S98
Author(s):  
M. Pompe-Novak ◽  
M. Tušek-Žnidarič ◽  
B. Štrukelj ◽  
M. Ravnikar
Keyword(s):  
Electron Microscopy ◽  
Solanum Tuberosum ◽  
Jasmonic Acid ◽  
Cell Walls ◽  
Cysteine Proteinase ◽  
Solanum Tuberosum L ◽  
Cell Types ◽  
Protein Bodies ◽  
Potato Plants

The localization of cysteine proteinase PLCP-2 was investigated in potato plants (Solanum tuberosum L.) cultivar Désirée by electron microscopy. Healthy and PVY<sup>NTN</sup> infected potato plants were grown in vitro on media with or without a supplement of jasmonic acid. We had already shown that PLCP-2 is present in leaves, stems, tips of shoots and tips of roots of healthy and PVY<sup>NTN</sup> infected plants. It was detected in various cell types in protein bodies in vacuoles, in cytoplasm and in cell walls. There were significantly larger amounts of PLCP-2 in plants grown on medium with a supplement of jasmonic acid in both healthy and virus infected plants. More protein bodies in vacuoles were found in plants grown on medium with addition of jasmonic acid.

Structural changes in whole milk during the production of sterile concentrates: an electron microscope study

1970 ◽  
Vol 37 (3) ◽  
pp. 513-522 ◽  
Author(s):  
P. W. Board ◽  
Joan M. Bain ◽  
D. W. Gove ◽  
J. T. Mullett
Keyword(s):  
Electron Microscopy ◽  
Structural Changes ◽  
Physical Stability ◽  
Protein Bodies ◽  
Large Protein ◽  
Casein Micelles ◽  
Fat Globules ◽  
Whole Milk ◽  
Freeze Dried ◽  
Average Size

SummaryElectron microscopy was used to study the effect of addition of NaOH, forewarming, homogenization, concentration, and heat sterilization on the structure of whole milk during the production of 4 heat-sterilized concentrates that showed different degrees of physical stability. The samples were prepared for electron microscopy by adding fixative either to liquid or freeze-dried material, and then embedding for sectioning.Noticeable structural changes occurred during forewarming of samples containing added NaOH, during homogenization, and during heat sterilization. Addition of NaOH and forewarming decreased the closeness of packing of the subunits in the casein micelles. Homogenization reduced the average size of the fat globules, and protein became attached to their surfaces. Heat sterilization caused coalescence of protein. In non-homogenized sterilized concentrate with added NaOH, protein bodies of about 100 times the volume of the original casein micelles were formed; these were free-floating and the concentrate was stable. In non-homogenized sterilized concentrate with no added NaOH the protein bodies were about 15 times the size of the casein micelles and bridged to each other, thereby forming a sediment consisting of large irregular particles. Very large protein bodies containing fat globules formed during heat sterilization of the homogenized samples, both in the presence and in the absence of NaOH, and were responsible for the formation of sediment in these 2 products.Needle crystals observed in most samples were identifed as CaCO3. H2O by selected area diffraction; KC1 crystals were also detected.

scholarly journals Amino Acid Sequencing and cDNA Cloning of Rice Seed Storage Proteins, the 13kDa Prolamins, Extracted from Type I Protein Bodies.

1999 ◽  
Vol 16 (2) ◽  
pp. 103-113 ◽  
Author(s):  
Norihiro MITSUKAWA ◽  
Ryoichi KONISHI ◽  
Kunitomo KIDZU ◽  
Kozo OHTSUKI ◽  
Takehiro MASUMURA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cdna Cloning ◽  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Bodies ◽  
Type I ◽  
Rice Seed ◽  
Amino Acid Sequencing

Occurrence of Globoid Crystals in Cotyledonary Protein Bodies of Pisum sativum as Influenced by Experimentally Induced Changes in Mg, Ca and K Contents of Seeds

1985 ◽  
Vol 12 (4) ◽  
pp. 341 ◽  
Author(s):  
JNA Lott ◽  
PJ Randall ◽  
DJ Goodchild ◽  
S Craig
Keyword(s):  
Electron Microscopy ◽  
Pisum Sativum ◽  
Energy Dispersive ◽  
Protein Bodies ◽  
Rare Occurrence ◽  
Review Of Literature ◽  
X Ray ◽  
K Concentration ◽  
Induced Changes ◽  
Experimentally Induced

In many species globoid crystals in protein bodies of seeds are very common while in other species they are rarely observed. A review of literature suggested that the balance between divalent (Mg2+ and Ca2+) and monovalent (K+) cations may be important in determining whether or not globoid crystals will form. To test this hypothesis, experiments were carried out to add Mg and Ca, or Ca alone, to pods developing on K-deficient pea plants. While it was possible to cause a reduction in K concentration and increases in Mg and Ca concentrations, any changes to the normal mineral storage pattern in pea cotyledons were remarkably small. In some treatments, statistically significant increases in the ratio (Mg + Ca)/K were obtained and the sample with the greatest increase was examined in detail by electron microscopy and energy dispersive X-ray analysis. In this sample globoid crystals were common, in contrast to their normally rare occurrence in pea cotyledonary tissue.

scholarly journals Transgenic rice seed expressing flavonoid biosynthetic genes accumulate glycosylated and/or acylated flavonoids in protein bodies

2015 ◽  
Vol 67 (1) ◽  
pp. 95-106 ◽  
Author(s):  
Yuko Ogo ◽  
Tetsuya Mori ◽  
Ryo Nakabayashi ◽  
Kazuki Saito ◽  
Fumio Takaiwa
Keyword(s):  
Transgenic Rice ◽  
Protein Bodies ◽  
Rice Seed ◽  
Biosynthetic Genes ◽  
Transgenic Rice Seed

scholarly journals Histochemical analysis of seed reserve mobilization in Passiflora edulis Sims fo. flavicarpa O. Deg. (yellow passion fruit) during germination

2011 ◽  
Vol 71 (3) ◽  
pp. 701-708 ◽  
Author(s):  
HH. Tozzi ◽  
M. Takaki
Keyword(s):  
Passion Fruit ◽  
Protein Bodies ◽  
Histochemical Analysis ◽  
Passiflora Edulis ◽  
Starch Grains ◽  
Reserve Mobilization ◽  
Germination Period ◽  
Radicle Protrusion ◽  
Passiflora Edulis Sims ◽  
Yellow Passion Fruit

In the present work, we analyzed the histochemical aspects of Passiflora edulis seeds reserve mobilization during the first ten days of germination. Our results showed that mainly lipids present in the endosperm are used as a reserve source, and their levels reduce at the same time the radicle protrudes, between the fourth and sixth day of sowing. Furthermore, protein bodies are present in the cotyledons, which are degraded as germination occurs and are almost depleted by the time of radicle protrusion. Starch grains also appear in the late germination period, and it is not clear if there is any reserve wall polysaccharide consumption in the endosperm.

Electron paramagnetic resonance and microstructural insights into the thermal behavior of simonkolleite nanoplatelets

2020 ◽  
Vol 22 (17) ◽  
pp. 9503-9512
Author(s):  
Arpad Mihai Rostas ◽  
Andrei Cristian Kuncser ◽  
Daniela Ghica ◽  
Alexandra Palici ◽  
Valentin Adrian Maraloiu ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Experimental Data ◽  
Thermal Decomposition ◽  
Electron Paramagnetic Resonance ◽  
Thermal Behavior ◽  
Decomposition Process ◽  
Thermal Decomposition Process ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

The thermal decomposition process of simonkolleite, at 500 °C was monitored by EPR and electron microscopy. The experimental data indicate that after an 1 h at 500 °C, three morphologies can be observed from the thermal decomposition of ZHC.

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