The Cytosome of differentiating Cells in the Ovotestes of Slugs

1951 ◽  
Vol s3-92 (20) ◽  
pp. 453-461
Author(s):  
D. PELLUET ◽  
ANNE H. G. WATTS

The distribution of ascorbic acid, alkaline phosphatase, and mitochondria has been followed during the differentiation of germinal epithelium cells into spermatogonia, oocytes, and nurse-cells in the ovotestes of slugs. All three substances appear in the cytoplasm of the oocyte and increase during its growth. Occasionally the oocyte nucleolus gives a positive test for ascorbic acid. The heads of the mature spermatozoa contain alkaline phosphatase. The cytoplasm of the germinal epithelium, spermatogonia, and spermatocytes occasionally gives a positive reaction for ascorbic acid. The development of the nurse-cells is accompanied by an increase in the size of the mitochondria. Attachment of the spermatids results in a decrease in size and number of the mitochondria in the nurse-cells. Alkaline phosphatase, ascorbic acid, and mitochondria show no significant change, either in form or quantity, in the indifferent cells of the ovotestis by which one could predict their destiny.

1960 ◽  
Vol 20 (3) ◽  
pp. 251-255 ◽  
Author(s):  
M. PEREK ◽  
A. EILAT

SUMMARY Injections of both fast- and long-acting adrenocorticotrophic hormone (ACTH) were followed by depletion of adrenal ascorbic acid (AA) in 3-week- and 6-week-old chicks when the bursa of Fabricius had been removed. The speed of depletion was similar to that known in mammals. Intact birds did not respond in this respect to ACTH treatment. A marked involution of the bursa of Fabricius occurred in chicks treated with prolonged-acting ACTH. A depletion of the total AA content of the bursa was noted, without any significant change in its concentration in the tissue of the gland. The results of the experiments indicate that the bursa of Fabricius is involved in preventing the release of adrenal AA after ACTH treatment.


1970 ◽  
Vol 16 (9) ◽  
pp. 776-780 ◽  
Author(s):  
Jesse F Goodwin

Abstract A direct method has been devised for determining serum and urinary inorganic phosphorus and serum phosphatase activity. Inorganic phosphorus forms a phosphomolybdate complex in the presence of borate. The complex is reduced with ascorbic acid. The resulting suspension is solubilized with carbonate and the absorbance measured at 720 nm. Samples containing low to moderate concentrations of bilirubin may be assayed by the method, and it compares favorably with a p-semidine reduction procedure with use of a TCA filtrate. Alkaline phosphatase values obtained by the method in which a β-glycerophosphate substrate is used compare favorably with a reference method in which p-nitrophenolphosphate is used as a substrate. Citrates, fluorides, nitrites, oxalates, and mannitol do not appreciably affect results obtained by the method.


2020 ◽  
Vol 321 ◽  
pp. 128511
Author(s):  
Shao-Bin He ◽  
Paramasivam Balasubramanian ◽  
Ai-Ling Hu ◽  
Xiao-Qing Zheng ◽  
Meng-Ting Lin ◽  
...  

Parasitology ◽  
1962 ◽  
Vol 52 (1-2) ◽  
pp. 153-157 ◽  
Author(s):  
A. B. Chowdhury ◽  
B. Dasgupta ◽  
H. N. Ray

There is histochemical evidence for the presence of calcium, glycogen, simple proteins and alkaline phosphatase in the calcareous corpuscles occurring in the parenchyma of Taenia saginata. A distinct Feulgen-positive reaction is seen in most of these corpuscles. The material yielding this positive reaction is apparently derived from the nucleus of certain mesenchymal cells from which these corpuscles supposedly originate. In some corpuscles, which are probably at the early stage of formation, the nucleus of such a mesenchymal cell is clearly seen adhering to the surface of the corpuscle. The identity of the nucleus of such cells is apparently lost in the fully formed corpuscle. Each corpuscle has a concentric appearance and is probably formed in successive layers.


Enzyme ◽  
1983 ◽  
Vol 30 (2) ◽  
pp. 145-148 ◽  
Author(s):  
G.A.D. Miggiano ◽  
A. Mordente ◽  
G.E. Martorana ◽  
E. Meucci ◽  
A. Castelli

Sign in / Sign up

Export Citation Format

Share Document