Ultrastructural localization of acid phosphatase activity in the small intestinal absorptive cells of adult rats

1979 ◽  
Vol 62 (2) ◽  
pp. 113-124 ◽  
Author(s):  
K. Ono
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Ultrastructural Localization ◽  
Adult Rats ◽  
Absorptive Cells ◽  
Small Intestinal

Acid phosphatase activity in Pinus pinea – Tuber albidum ectomycorrhizal association

1992 ◽  
Vol 70 (7) ◽  
pp. 1377-1383 ◽  
Author(s):  
S. Pasqualini ◽  
F. Panara ◽  
M. Antonielli
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Middle Lamella ◽  
Ultrastructural Localization ◽  
Ectomycorrhizal Fungus ◽  
Pinus Pinea ◽  
Inorganic Pyrophosphate ◽  
Mycorrhizal Roots ◽  
Substrate Concentrations

Acid phosphatase activity of pine (Pinus pinea L.) roots was investigated in the presence or absence of the ectomycorrhizal fungus Tuber albidum Pico. Acid phosphatase activity was higher in mycorrhizal roots than in roots of uncolonized control plants. The optimum pH values for acid phosphatase were 3.5 and 5.0 for mycorrhizal roots and 5.0 for control roots. The acid phosphatase activity was inhibited by tartrate, fluoride, and molybdate ions, but a lower inhibition was exerted by orthophosphate. Mycorrhizal roots of pine possessed active acid phosphatases that hydrolyzed a wide variety of natural and synthetic phosphate esters. In particular, the enzyme was active against phytate and inorganic pyrophosphate. Two different Km values were estimated: about 0.22 mM and 2.78 mM at low and high substrate concentrations, respectively. The ultrastructural localization of acid phosphatase in mycorrhizal roots showed that the activity in the Hartig net was mainly localized in the plasmalemma of hyphae. Some lead phosphate precipitates were also observed in the middle lamella of the host cell. Key words: Pinus pinea, Tuber albidum, acid phosphatase, ectomycorrhiza, histochemical localization.

ULTRASTRUCTURAL LOCALIZATION OF A CHARACTERISTIC ACID PHOSPHATASE IN GRANULES OF RABBIT BASOPHILS

1974 ◽  
Vol 22 (12) ◽  
pp. 1092-1104 ◽  
Author(s):  
ATSUSHI KOMIYAMA ◽  
SAMUEL S. SPICER
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Potential Role ◽  
Strong Acid ◽  
Ultrastructural Localization ◽  
Buffy Coat ◽  
Cytoplasmic Granules ◽  
Nitrophenyl Phosphate ◽  
Tris Maleate

Bone marrow basophils incubated in Gomori medium at pH 6.0-6.8 exhibited strong acid phosphatase activity suggestive of a potential role in endocytosis in one-third of the cytoplasmic granules and also in Golgi elements. Buffy coat basophils contained about one-third as many reactive granules. Reaction product was confined to the threadlike component of the larger granules predominant in early basophils and was absent from the denser-type granules predominant in late basophils. In centrioles of basophils acid phosphatase appeared localized between triplet fibers. Reactivity with the Gomori medium was diminished at pH 5.0, absent at pH 8.0 and only slightly decreased with p-nitrophenyl phosphate as substrate. Basophils incubated in Barka-Anderson medium at pH 5.0-6.8 revealed light acid phosphatase activity in the Golgi lamellae but essentially none in cytoplasmic granules. Tris-maleate buffer of the Barka-Anderson medium replacing the sodium acetate of the Gomori medium inhibited the reactivity in the granules. Incubation in media containing NaF, or lacking substrate, eliminated the heavy precipitates in granules and Golgi elements but yielded light, nonenzymatic lead staining in Golgi and tubulovesicular structures and atypical granules present only in buffy coat basophils.

scholarly journals Ultrastructural localization of acid phosphatase activity in the kidney sac nephrocytes of helix aspersa.

1984 ◽  
Vol 17 (4) ◽  
pp. 371-377 ◽  
Author(s):  
INMACULADA SÁNCHEZ-AGUAYO ◽  
JOSEFINA HIDALGO ◽  
FELIPE CORTES ◽  
JOSE LUIS LÓPEZ-CAMPOS
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Ultrastructural Localization ◽  
Helix Aspersa

A comparison of the effects of castration and 6-methylene progesterone, a 5α-reductase inhibitor, on the rat ventral prostate

1987 ◽  
Vol 65 (7) ◽  
pp. 626-634 ◽  
Author(s):  
Sherry A. Marts ◽  
George M. Padilla ◽  
Vladimir Petrow
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Reductase Activity ◽  
Prostatic Acid Phosphatase ◽  
Serum Levels ◽  
Ventral Prostate ◽  
Absolute Amount ◽  
Adult Rats

6-Methylene progesterone (6MP) is an irreversible in vitro kcat inhibitor of rat prostate 5α-reductase, the enzyme which converts testosterone (T) to dihydrotestosterone (DHT). Treatment of adult rats with 6MP or diethylstilbestrol (DES) decreased the weight of the ventral prostate (VP) by 45%, while castration reduced it by 86%. Histologically, the 6MP-treated VP were indistinguishable from those of controls, while the VP from DES-treated rats showed fibrous stromal hypertrophy as in castrated rats. The prostatic hydroxyproline content, an index of collagen levels, was enhanced by castration or DES, but was not significantly increased by 6MP. Within 2 days of 6MP treatment, the 5α-reductase activity was reduced by 46% and ornithine decarboxylase (ODC) activity was lowered by 27%. During this time the prostatic acid phosphatase activity increased 42% and remained elevated with continued exposure to 6MP up to 13 days. The castration-induced involution of the VP was accompanied by a reduction in serum T and an increase in serum luteinizing hormone (LH). 6MP had no effect on T and LH serum levels but reduced the DHT content within the VP by 64%. Our results indicate that the structure and secretory acid phosphatase activity of the VP are less sensitive to changes in the ratio of T: DHT than is cell proliferation. Thus, the relative amounts of DHT and T within the VP may prove to be more significant than the absolute amount of either androgen in controlling prostate growth or its attendant neoplasms.

ACID PHOSPHATASE ACTIVITY IN THE PANCREATIC ISLETS OF RATS OF DIFFERENT AGES

1962 ◽  
Vol 40 (4) ◽  
pp. 604-612 ◽  
Author(s):  
Claes Hellerström ◽  
Sven Brolin ◽  
Stig Larsson ◽  
Bo Hellman
Keyword(s):  
Acid Phosphatase ◽  
Pancreatic Islets ◽  
Phosphatase Activity ◽  
Islets Of Langerhans ◽  
Acid Phosphatase Activity ◽  
Early Stage ◽  
Postnatal Life ◽  
Adult Rats ◽  
Different Ages ◽  
Acid Phosphatase Reaction

ABSTRACT Histochemical methods for acid phosphatase and glucose-6-phosphatase were applied to the islets of Langerhans in rats of different ages. It was not possible to demonstrate any specific glucose-6-phosphatase activity, since at the pH optimum of this enzyme, both glucose-6-phosphate and sodium-β-glycerophosphate were hydrolyzed; the more intense reaction occurring with the latter substrate. At the end of the intrauterine life there was a marked acid phosphatase reaction, which appeared unchanged during the first 10 days of postnatal life but was considerably weaker in adult rats. The occurrence of a smaller number of non-reacting cells in the islet periphery was assumed to be evidence that there was no demonstrable acid phosphatase activity in one or both types of A cells. The considerable reaction found in the islets of foetuses and young rats might reflect the maturation and rapid proliferation of these cells during early stage of life.

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