Fine Structural Localization of Acid Phosphatase and Aryl Sulfatase Activities in the Intermediate Layer of Hymenolepis diminuta Cysticercoids

1969 ◽  
Vol 88 (3) ◽  
pp. 411 ◽  
Author(s):  
Burton J. Bogitsh
Keyword(s):  
Acid Phosphatase ◽  
Intermediate Layer ◽  
Hymenolepis Diminuta ◽  
Structural Localization ◽  
Aryl Sulfatase

Cytochemical study of lysosomal aryl sulfatase and acid phosphatase activities in rat retina

Micron (1969) ◽  
1979 ◽  
Vol 10 (3) ◽  
pp. 187-188
Author(s):  
Edward Essner ◽  
Gregg M. Gorrin ◽  
Richard A. Griewski
Keyword(s):  
Acid Phosphatase ◽  
Cytochemical Study ◽  
Aryl Sulfatase ◽  
Rat Retina ◽  
Phosphatase Activities

scholarly journals THE DEMONSTRATION OF ACID HYDROLASE ACTIVITIES IN THE INCLUSION BODIES OF TYPE II ALVEOLAR CELLS AND OTHER LYSOSOMES IN THE RABBIT LUNG

1968 ◽  
Vol 16 (2) ◽  
pp. 102-109 ◽  
Author(s):  
SIDNEY GOLDFISCHER ◽  
YUTAKA KIKKAWA ◽  
LEE HOFFMAN
Keyword(s):  
Acid Phosphatase ◽  
Inclusion Bodies ◽  
Active Sites ◽  
Cytoplasmic Inclusion ◽  
Alveolar Epithelial Cells ◽  
Type Ii ◽  
Alveolar Cells ◽  
Rabbit Lung ◽  
Aryl Sulfatase ◽  
Alveolar Epithelial

Type II alveolar epithelial cells show high levels of acid phosphatase, aryl sulfatase B and β-glucuronidase activities. In formalin- and glutaraldehyde-fixed rabbit lung acid phosphatase and aryl sulfatase B activities were demonstrated in the cytoplasmic inclusion bodies, supporting their identification as lysosomes. Type II cells differ from alveolar macrophages in their levels of hydrolase activity and the fine structure of their active sites.

scholarly journals Fine Structural Localization of Acid Phosphatase Activity in Myeloma Cells

1968 ◽  
Vol 96 (4) ◽  
pp. 399-403 ◽  
Author(s):  
Akira B. Miura ◽  
Atsuo Suzuki ◽  
Seiju Onodera ◽  
Shinobu Sakamoto ◽  
Chiyuki Suzuki ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Structural Localization ◽  
Myeloma Cells

scholarly journals ENZYME HISTOCHEMISTRY OF BONE INDUCTION BY URINARY BLADDER EPITHELIUM

1965 ◽  
Vol 13 (4) ◽  
pp. 255-264 ◽  
Author(s):  
SHOHEI KAGAWA
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Urinary Bladder ◽  
Intermediate Layer ◽  
Succinic Dehydrogenase ◽  
Basal Layer ◽  
Oxidative Enzymes ◽  
Bladder Epithelium ◽  
Malic Dehydrogenase ◽  
Normal Bladder

Homogenous transplants of urinary bladder mucosa were made in guinea pigs, and induced bone formation was observed histochemically for alkaline phosphatase, acid phosphatase, esterase, β-glucuronidase, aminopeptidase, and oxidative enzymes, i.e., succinic dehydrogenase, diphosphopyridine nucleotide-dependent dehydrogenase (lactate, malate, glutamate, α-glycerophosphate, β-hydroxybutyrate) and triphosphopyridine nucleotide-dependent dehydrogenase (glucose-6-phosphate and isocitrate). Normal urinary bladder epithelium contained intense alkaline phosphatase and slight acid phosphatase activity throughout. There was weak esterase activity in intermediate layer and weak β-glucuronidase activity in intermediate layer. Succinic dehydrogenase was present throughout the epithelium, and was most active in the basal layer. Lactic and malic dehydrogenase activities were intense. Glutamic, α-glycerophosphate and β-hydroxybutyric dehydrogenase activities were low, but glucose-6-phosphate and isocitric dehydrogenase activities were high. In the initial stage after transplantation, alkaline phosphatase, aminopeptidase and lactic dehydrogenase appeared in the connective tissue surrounding the transplanted mucosa in association with an inflammatory infiltration. Epithelial transplants formed cysts. Lactic, malic and triphosphopyridine nucleotide-dependent dehydrogenases in cystic epithelium were as intense as in normal bladder, though other enzymes decreased. Hyaline formation occurred around the cyst. No appreciable enzyme activity was demonstrated in this hyalinized portion, but when bone appeared marked activity of alkaline and acid phosphatases was seen around it. Histochemical patterns in the induced bone were essentially the same as in normal bone.

scholarly journals FINE STRUCTURAL LOCALIZATION OF ACID AND ALKALINE PHOSPHATASES IN CELLS OF RABBIT BLOOD AND BONE MARROW

1967 ◽  
Vol 15 (6) ◽  
pp. 311-334 ◽  
Author(s):  
B. K. WETZEL ◽  
S. S. SPICER ◽  
R. G. HORN
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Mononuclear Cells ◽  
Nuclear Staining ◽  
Alkaline Phosphatases ◽  
Structural Localization ◽  
Dense Granules ◽  
Dense Bodies

In rabbit heterophils, acid phosphatase activity occurs in primary (azurophil) granules which predominate in early cells and persist in mature cells and in tertiary granules which are seen only in mature cells. Alkaline phosphatase activity occurs in secondary granules which appear in intermediate heterophils and later predominate in mature cells. Acid phosphatase activity in heterophil Golgi zones coincides developmentally with the genesis of primary and, later, tertiary granules, whereas alkaline phosphatase in the Golgi complex coincides with secondary granulogenesis. In developing eosinophils, acid phosphatase reaction product occurs in Golgi elements, rims the spherical precursors of angular, mature granules and appears inconsistently within mature granules. Basophil myelocytes show acid phosphatase in Golgi elements but not in specific granules. Additional acid phosphatase reactive structures include: granules of mononuclear cells; phagocytic vacuoles in macrophages; autophagic vacuoles in maturing erythroid cells; small dense granules of platelets; dense bodies in lipocytes; and Golgi elements of mononuclear cells, macrophages, nucleated red cells, megakaryocytes and lipocytes. Localized deposits were absent in control specimens except for enzyme-independent nuclear staining in alkaline phosphatase preparations.

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