The light and electron microscopic distribution of acid phosphatase activity in human normal oesophageal epithelium

1978 ◽  
Vol 10 (2) ◽  
pp. 159-170 ◽  
Author(s):  
D. Hopwood ◽  
Kathleen R. Logan ◽  
G. Milne
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Electron Microscopic ◽  
Microscopic Distribution

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.

scholarly journals Electron microscopic cytochemical studies on acid phosphatase activity in acute myocardial ischemia.

1983 ◽  
Vol 24 (4) ◽  
pp. 595-606 ◽  
Author(s):  
Naomi NAKAMURA ◽  
Yasufumi SASAI ◽  
Youichi TAKEYAMA ◽  
Takashi KATAGIRI
Keyword(s):  
Acid Phosphatase ◽  
Myocardial Ischemia ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Acute Myocardial Ischemia ◽  
Electron Microscopic

scholarly journals CENTRIFUGAL, BIOCHEMICAL, AND ELECTRON MICROSCOPIC ANALYSIS OF CYTOPLASMIC PARTICULATES IN LIVER HOMOGENATES

1956 ◽  
Vol 2 (1) ◽  
pp. 33-54 ◽  
Author(s):  
Edward L. Kuff ◽  
George H. Hogeboom ◽  
Albert J. Dalton
Keyword(s):  
Electron Microscopy ◽  
Acid Phosphatase ◽  
Cytochrome C ◽  
Size Distribution ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Reductase Activity ◽  
Size Group ◽  
Average Radius ◽  
Electron Microscopic

A combined centrifugal, biochemical, and electron microscopic study of the cytoplasmic particulates present in 0.88 M sucrose homogenates of rat liver has been carried out. Size distribution analyses of particles containing pentose nucleic acid (PNA) and exhibiting several types of enzymatic activity revealed three major size groups within the range of particle radius between 10 and 500 mµ. A different array of biochemical properties was associated with each size group. The largest particles, with an average radius (assuming spherical shape) in the region of 220 to 260 mµ, contained all of the succinic dehydrogenase activity of the cytoplasmic extract, 29 per cent of the diphosphopyridine nucleotide (DPN)-cytochrome c reductase activity, and minor amounts of PNA and acid phosphatase activity. Cytologically, this group of particles was identified with the mitochondria. All of the uricase activity, 58 per cent of the acid phosphatase activity, and 26 per cent of the PNA was apparently associated with a second size group of particles (average radius 120 mµ) which were tentatively identified by electron microscopy with vesicular structures derived from the ergastoplasm of the intact cell. The third particle group demonstrated by centrifugation exhibited a major size distribution peak at 25 mµ and a second smaller peak at 55 mµ. Over 50 per cent of the total cytoplasmic PNA and DPN-cytochrome c reductase activity was associated with particles in this size group. Electron microscopy revealed a morphologically heterogeneous population of particles within this size range.

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