Localization of gibberellic acid-induced acid phosphatase activity in the endoplasmic reticulum of barley aleurone cells with the electron microscope

Planta ◽  
1979 ◽  
Vol 147 (2) ◽  
pp. 134-140 ◽  
Author(s):  
N. A. Pyliotis ◽  
A. E. Ashford ◽  
M. I. Whitecross ◽  
J. V. Jacobsen
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Acid Phosphatase ◽  
Gibberellic Acid ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Aleurone Cells ◽  
Barley Aleurone

scholarly journals DIAZOPHTHALOCYANINS AS REAGENTS FOR FINE STRUCTURAL CYTOCHEMISTRY

1965 ◽  
Vol 25 (1) ◽  
pp. 23-41 ◽  
Author(s):  
Lois Withrow Tice ◽  
Russell J. Barrnett
Keyword(s):  
Electron Microscope ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Alcian Blue ◽  
Azo Dyes ◽  
Acid Phosphatase Activity ◽  
Fixed Material

This paper reports the synthesis of 14 diazophthalocyanins containing Mg, Cu, or Pb as the chelated metal. To assess the usefulness of these compounds for fine structural cytochemistry, the relative coupling rates with naphthols were tested as well as the solubility of the resulting azo dyes. Three of the diazotates were reacted with tissue proteins in aldehyde-fixed material, and the density increases thus produced were compared in the electron microscope with those produced by staining similarly fixed material with the phthalocyanin dye, Alcian Blue. Finally, one of the diazotates was used as a capture reagent for the demonstration of the sites of acid phosphatase activity with the electron microscope.

scholarly journals CYTOLOGICAL STUDIES ON TWO FUNCTIONAL HEPATOMAS

1962 ◽  
Vol 15 (2) ◽  
pp. 289-312 ◽  
Author(s):  
Edward Essner ◽  
Alex B. Novikoff
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Secretory Granules ◽  
Dynamic State ◽  
Secretory Product ◽  
Electron Microscopic ◽  
Golgi Membranes

The Reuber hepatoma H-35 and Morris hepatoma 5123 have been studied by electron microscopy and by cytochemical staining methods for a number of phosphatases. These studies emphasize the resemblances of the two tumors to rat liver, but they also indicate distinctive features in each of the three tissues. Secretory product accumulates within the cisternae of the Golgi apparatus that dilate to form the Golgi vacuoles. The vacuoles apparently separate, and secretory material undergoes further condensation within them. These "secretory vacuoles" possess acid phosphatase activity and may thus be considered lysosomes. The membranes of the Golgi apparatus are without acid phosphatase activity but show high levels of thiaminepyrophosphatase activity. The endoplasmic reticulum also hydrolyzes thiaminepyrophosphate but at a lower rate; it hydrolyzes the diphosphates of uridine, guanosine, and inosine rapidly. These observations and the electron microscopic images are consistent with the view that the cytomembranes are in a dynamic state of flux, movement, and transformation in the living cell, and that smooth surfaced derivatives of the endoplasmic reticulum become refashioned into the Golgi membranes as the Golgi membranes are being refashioned into those that delimit secretory vacuoles. The variations encountered in the two hepatomas are described. The electron microscope literature dealing with the relations of the Golgi apparatus to secretory granules, on the one hand, and the endoplasmic reticulum, on the other, is reviewed briefly.

Cellular mechanisms of periostracum formation in Physa spp. (Mollusca: Pulmonata)

1978 ◽  
Vol 56 (11) ◽  
pp. 2299-2311 ◽  
Author(s):  
G. M. Jones ◽  
A. S. M. Saleuddin
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rough Endoplasmic Reticulum ◽  
Acid Phosphatase Activity ◽  
Homogeneous Material ◽  
Cellular Mechanisms ◽  
Phenoloxidase Activity ◽  
Enzyme Substrate ◽  
Mantle Edge

The periostracum comprises an external lamella, 13 nm thick, and one sublamellar layer. Periostracal cells secrete the lamella as preformed periostracal units. The mantle edge gland (meg) produces most of the sublamellar layer. A sequence of formation of periostracal units within the periostracal cells is suggested. Homogeneous inclusions, possibly Golgi derived, fuse into larger, irregular inclusions. Within these inclusions, three-layered membranes, 7 nm thick, arise from the homogeneous material. The membranes fuse in pairs to form the five-layered, 13-nm periostracal units. Acid phosphatase activity has been localised al the surfaces of the periostracal units and might be involved in modifying the units prior to their discharge. Phenoloxidase and polyphenols have been localised in the meg, suggesting that this region is responsible for periostracal sclerotisation. Phenoloxidase activity is present in Golgi, rough endoplasmic reticulum, and apical secretory inclusions in cells in the anterior two-thirds of the meg. Polyphenols are present in apical secretory inclusions, particulary in three or four cells in the posterior meg. This distribution may suggest that phenoloxidase is incorporated into all levels of the sublamellar layer and that sclerotisation occurs subsequently when the enzyme substrate is presented.

scholarly journals Amylase and acid phosphatase activity in potato tubers treated with gibberellic acid and stored at 2°C and 8°C

2015 ◽  
Vol 30 (1) ◽  
pp. 95-101 ◽  
Author(s):  
M. Bielińska-Czarnecka ◽  
K. Białek
Keyword(s):  
Acid Phosphatase ◽  
Gibberellic Acid ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Amylase Activity ◽  
Amylolytic Activity ◽  
Potato Tubers ◽  
Two Peaks

Amylase activity was higher in tubers stored at 2°C and mare marked in the soaked ones (both in water and in GA<sub>3</sub>). In the late and difficult-sprouting cv. Uran, sokaing resulted in increased amylolytic activity also at 8°C stored tubers. On the contrary, the acid phosphatase activity was a little higher at 8°C than at 2°C stored tubers. At the former temperature two peaks of activity were marked:, in November–December and February–March.

The host-parasite interface of Cyathocotyle bushiensis Khan, 1962 (Trematoda: Strigeoidea)

Parasitology ◽  
1968 ◽  
Vol 58 (2) ◽  
pp. 371-375 ◽  
Author(s):  
David A. Erasmus
Keyword(s):  
Electron Microscope ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Plasma Membranes ◽  
Science Research ◽  
Strong Acid ◽  
Gland Cells ◽  
Adhesive Organ ◽  
Cyathocotyle Bushiensis

A combination of histochemical and electron microscope techniques have demonstrated, in Cyathocotyle bushiensis, alkaline phosphatase activity in the matrix of the tegument, in the distal and basal plasma membranes of the tegument, in the wall of the ducts extending from the adhesive organ gland cells and in the wall of the adhesive organ microvilli. Acid phosphatase activity was much stronger and was present in the tegument matrix and in the granular component of the secretion from the adhesive organ gland cells. Strong acid phosphatase activity was also present in the cisternae of the endoplasmic reticulum of the adhesive organ gland cells.I am greatly indebted to Professor Brough for the excellent facilities available within this department. I also wish to thank Professor J. Sinclair (Department of Mining) for electron microscope facilities extended to me in the early stages of this investigation, and to Mr W. Henderson, Mr T. Davies and Miss M. Williams for their invaluable assistance. The purchase of the Huxley ultramicrotome, coating unit and an AEI EM 6 electron microscope was made possible by a grant from the Science Research Council.

Ébauches intracytoplasmiques de grains protéiques dans des cotylédons de Raphanus en développement

1986 ◽  
Vol 64 (12) ◽  
pp. 2887-2895
Author(s):  
Louis Genevès ◽  
Jacques Rutin
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rough Endoplasmic Reticulum ◽  
Early Phase ◽  
Acid Phosphatase Activity ◽  
Early Stage ◽  
Protein Bodies ◽  
Meristematic Cells ◽  
Size And Structure

Protein bodies were characterized at an early stage of their maturation in thin green cotyledons of developing radish embryos. They appeared as granules in the cytoplasm of meristematic cells. Their diameter (0.5 to 1 μm) was in the range of that of mitochondria. They were distinguished from vacuoles by their morphology, size, and structure. Some appeared to be associated with cisternae of endoplasmic reticulum or dictyosomes (permanganic fixations). Their evolution was synchronous in the cell and also in the cotyledonary tissue. Compact in appearance, they were constituted of thin packed fibrillar structures, limited by a denser peripheral layer. It is difficult to know whether or not they had a limiting membrane. Some possessed thin dense crystals or globoids (aldehydic fixations). During this early phase, several types of organelles seemed to contribute to the development of protein bodies, including saccules of rough endoplasmic reticulum and dictyosomes. Polyribosomes constituted a network around their surface. They did not exhibit any acid phosphatase activity. In this respect, they differed from the vacuoles, saccules of endoplasmic reticulum, and several neighbouring vesicles.

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