CHANGES IN HYDROLASE ENZYMORPHOLOGY OF RAT UTERUS AND VAGINA AFTER ESTROGENS; NAPHTHOL AS SUBSTRATES

1964 ◽  
Vol 12 (12) ◽  
pp. 908-918 ◽  
Author(s):  
KEIICHI WATANABE ◽  
WILLIAM H. FISHMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Enzyme Hydrolysis ◽  
Estrogen Treatment ◽  
Capillary Endothelium ◽  
Nonspecific Esterase ◽  
Rat Uterus ◽  
New Findings ◽  
Estradiol 17Β ◽  
Estrogen Administration

The early enzymorphologic changes of rat uterus and vagina on castration and following estrogen administration (estradiol-17β, estrone and estriol) were examined with regard to alkaline phosphatase, esterase, β-glucuronidase and acid phosphatase using naphthol AS compounds as substrates. Castration caused a marked decrease of enzyme activities except for alkaline phosphatase of capillary endothelium and for nonspecific esterase. All activities, compared to castrated controls, were markedly increased by estrogen administration except for the alkaline phosphatase of capillary endothelia. Estriol and estrone were more potent than estradiol-17β in the early stage of estrogen treatment (4-hour interval). The response of alkaline phosphatase of striated border of lumenal uterine epithelium to estrogen treatment is unique in that the other hydrolases were absent from this site. The estrogen sensitivity of the hydrolases of connective tissue cells of rat uterine stroma is clearly evident for the first time. Of interest also is a comparison of β-glucuronidase and acid phosphatase in which naphthol AS-BI is the product of enzyme hydrolysis in each case. Although the intensity of the respective staining reactions correlated well with each other in relation to the events of castration and estrogen administration, there were clear differences evident. Finally, the new findings demonstrate the value of the improved techniques as well as resolve some ambiguities of earlier findings obtained with diverse methods.

A study of the distribution of acid and alkaline phosphatase in the genital tract of the Zebu bull (Bos indicus)

1954 ◽  
Vol 45 (2) ◽  
pp. 173-178 ◽  
Author(s):  
D. H. L. Rollinson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Positive Reaction ◽  
Reproductive Tract ◽  
Vas Deferens ◽  
Bos Indicus ◽  
Seminal Vesicles ◽  
Capillary Endothelium ◽  
Cellular Reaction ◽  
Spermatogenic Epithelium

The histochemical localization of acid and alkaline glycerophosphatase (phosphomonoesterase) has been determined throughout the reproductive tract in the bull. Sections were incubated in a buffer substrate containing sodium β-glycerophosphate at pH 4·5 and pH 9·4. Duplicate sections were incubated for progressive lengths of time ranging from ½ hr. (alkaline phosphatase) to a maximum of 48 hr. (acid phosphatase).Evidence of the presence of both enzymes has been obtained in the tissues which compose the reproductive tract. In the case of acid phosphatase the reaction was predominant in the nuclei of the lining epithelial cells. In addition, a positive cellular reaction was found in the distal portions of the epithelium lining the epididymis, the ampulla of the vas deferens and the seminal vesicles. The reaction obtained in the testis appeared to vary with the stage of activity of the tubule.In the case of alkaline phosphatase the reaction was predominantly shown by the basement membrane and the capillaries throughout the tissues with a cellular reaction in the distal portions of the cells lining the epididymis, the ampulla of the vas deferens and the seminal vesicles. In the seminal vesicles the type ‘A’ cells reacted strongly while the periphery of the osmic staining vacuoles of the type ‘B’ cells also gave a positive reaction. The only activity present in the prostate was in the capillary endothelium. The spermatogenic epithelium showed a positive reaction, but no reaction was given by the interstitial cells.

Mucosal Histochemistry in Secretory Otitis

1975 ◽  
Vol 84 (1) ◽  
pp. 112-116 ◽  
Author(s):  
Tauno Palva ◽  
Antti Palva
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Biochemical Analysis ◽  
Secretory Cells ◽  
Nonspecific Esterase ◽  
Positive Staining ◽  
Secretory Otitis Media ◽  
Intercellular Substance ◽  
Glue Ear ◽  
Glandular Structures

Mucosal biopsies were taken from 20 ears with secretory otitis media (glue ear) and histochemical stainings were made for comparison with data obtained from biochemical analysis of the fluids. Acid phosphatase, lactate dehydrogenase (LD), and malate dehydrogenase (MD), the activity of which in the ear fluids was 20 to 30 times higher than in serum, were found to appear as strong precipitates in the middle ear epithelium, particularly in the top layer. Alkaline phosphatase activity was only exceptionally seen in the epithelium but appeared in the capillaries and histiocytes. Nonspecific esterase appeared irregularly in the epithelium and regularly in histiocytes. The latter two had lower activities in ear fluids than in serum. Epithelial secretory cells and subepithelial glands and cysts showed strong alcian blue (AB)-positive staining. Positive material appeared also in the cytoplasm of the epithelial cells and in the intercellular substance. Distinct PAS-positive staining appeared in the columnar epithelium and particularly in the free mucus on top of the epithelium but was less pronounced in the glandular structures and absent from the cysts.

Effects of Kanwa on Rat Gastrointestinal Phosphatases

2010 ◽  
Vol 3 (3) ◽  
pp. 1147-1152
Author(s):  
Jacob Bamaiyi ◽  
Omajali ◽  
Sanni Momoh
Keyword(s):  
Alkaline Phosphatase ◽  
Small Intestine ◽  
Acid Phosphatase ◽  
Sodium Carbonate ◽  
Elevated Level ◽  
Food Additive ◽  
Alkaline Phosphatases ◽  
Acid And Alkaline Phosphatases ◽  
Diagnostic Indices ◽  
High Level

This study investigates the effects of kanwa on rat gastrointestinal phosphatases. The rats were administered 7% w/v concentration of  trona (Kanwa) orally for a period of two weeks in order to investigate how this compound is being used as food additive in some homes in Nigeria. The Kanwa used in this study was the handpicked variety obtained from sellers from Anyigba market in eastern part of Kogi State, Nigeria. Kanwa, a hydrated sodium carbonate (Na2CO3NaHCO3.2H2O) was obtained as a dried lake salt. Acid phosphatase has the ability to dephosphorylate molecules containing phosphate group. The decreased and elevated level in serum or plasma acid and alkaline phosphatases serves as diagnostic indices for various diseases. Results showed that there was increase and decrease of acid phosphatase (ACP) activities in both the stomach and small intestine. The activities of alkaline phosphatase (ALP) fluctuated in the small intestine. However, in the stomach, an increase activity of ALP was noticed throughout the period of ‘Kanwa’ administration. We concluded that although the level of ‘Kanwa’ consumed in most homes may not be toxic if not taken continuously or repeatedly. Thus, continuous consumption should be discouraged as accumulation of high level of ‘Kanwa’ may cause damages or injuries to the various organs/tissues and may disrupt normal body function.

scholarly journals Bone-Derived Serum Enzymes and Bone Density in Perimenopausal Caucasian Women

1993 ◽  
Vol 30 (2) ◽  
pp. 191-194 ◽  
Author(s):  
J D Johnston ◽  
S Koneru ◽  
T Kuwana ◽  
S B Rosalki
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Bone Density ◽  
Femoral Neck ◽  
Serum Levels ◽  
Bone Alkaline Phosphatase ◽  
Serum Enzymes ◽  
Tartrate Resistant Acid Phosphatase ◽  
Vertebral Bone ◽  
Caucasian Women

Serum levels of bone-origin alkaline phosphatase and of tartrate-resistant acid phosphatase were measured in Caucasian women aged 41–69 years who had volunteered for bone densitometry. Bone alkaline phosphatase and tartrate-resistant acid phosphatase were inversely correlated with vertebral bone density and with femoral neck bone density. Bone alkaline phosphatase and acid phosphatase were also significantly correlated, consistent with the concept of ‘coupling’ between osteoblast and osteoclast activity.

scholarly journals Enzyme Histochemical Studies of Adipose Tissue in Porcine Yellow Fat Disease

1974 ◽  
Vol 11 (6) ◽  
pp. 465-476 ◽  
Author(s):  
L. H. J. C. Danse ◽  
W. A. Steenbergen-Botterweg
Keyword(s):  
Enzyme Activity ◽  
Adipose Tissue ◽  
Acid Phosphatase ◽  
Nonspecific Esterase ◽  
Cell Structures ◽  
Increased Activity

Adipose tissue of piglets with yellow fat disease had increased activity of nonspecific esterase, 5-nucleotidase, and acid phosphatase. Since these enzymes are associated with different cell structures and damage to these structures can result in increased enzyme activity, they are criteria for pathogenetic study of yellow fat disease.

scholarly journals Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture

1972 ◽  
Vol 127 (1) ◽  
pp. 87-96 ◽  
Author(s):  
P. G. Bolton ◽  
A. C. R. Dean
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Continuous Culture ◽  
Activity Profile ◽  
Glucose Effect ◽  
Ph Values ◽  
Nitrophenyl Phosphate ◽  
Wide Range ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

1. Phosphatase synthesis was studied in Klebsiella aerogenes grown in a wide range of continuous-culture systems. 2. Maximum acid phosphatase synthesis was associated with nutrient-limited, particularly carbohydrate-limited, growth at a relatively low rate, glucose-limited cells exhibiting the highest activity. Compared with glucose as the carbon-limiting growth material, other sugars not only altered the activity but also changed the pH–activity profile of the enzyme(s). 3. The affinity of the acid phosphatase in glucose-limited cells towards p-nitrophenyl phosphate (Km 0.25–0.43mm) was similar to that of staphylococcal acid phosphatase but was ten times greater than that of the Escherichia coli enzyme. 4. PO43−-limitation derepressed alkaline phosphatase synthesis but the amounts of activity were largely independent of the carbon source used for growth. 5. The enzymes were further differentiated by the effect of adding inhibitors (F−, PO43−) and sugars to the reaction mixture during the assays. In particular, it was shown that adding glucose, but not other sugars, stimulated the rate of hydrolysis of p-nitrophenyl phosphate by the acid phosphatase in carbohydrate-limited cells at low pH values (<4.6) but inhibited it at high pH values (>4.6). Alkaline phosphatase activity was unaffected. 6. The function of phosphatases in general is discussed and possible mechanisms for the glucose effect are outlined.

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