Ultrastructure of the ventriculus of the honey bee, Apis mellifera (L.): cytochemical localization of acid phosphatase, alkaline phosphatase, and nonspecific esterase

1990 ◽  
Vol 261 (3) ◽  
pp. 431-443 ◽  
Author(s):  
Desmond R. Jimenez ◽  
Martha Gilliam
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Apis Mellifera ◽  
Honey Bee ◽  
Nonspecific Esterase ◽  
Cytochemical Localization ◽  
Phosphatase Alkaline

scholarly journals Cytochemical localization of certain hydrolytic enzymes at various stages of development of Achlya flagellata mycelium

2015 ◽  
Vol 41 (2) ◽  
pp. 265-282 ◽  
Author(s):  
I. Palczewska ◽  
G. Jagodzka
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Azo Dyes ◽  
Acid Phosphatase Activity ◽  
Hydrolytic Enzymes ◽  
Cytochemical Localization ◽  
Cytoplasmic Granules ◽  
End Products ◽  
E 600 ◽  
Phosphatase Alkaline

The standard coupling azo dyes techniques were used to reveal the activities of acid phosphatase, alkaline phosphatase, esterase and β-galactoidase in the vegetative and reproductive cycle of <i>Achlya flagellata</i>. The end-products of the enzymic reactions, with the exception of E 600 sentisive esterese, which is localized in cytoplasm, occured in cytoplasmic granules. These granules are expected to be spherosomes. Acid phosphatase activity is high in differentiating sporangia, in antheridial hyphae and in degenerating oospheres where hydrolytic processes occur. β-galactosidase is the least active enzyme in the mycelium of <i>Achlya</i>.

SIGNIFICANCE OF TRANSAMINASE ACTIVITY OF SERUM

PEDIATRICS ◽  
1959 ◽  
Vol 24 (3) ◽  
pp. 360-361
Author(s):  
SAMUEL P. BESSMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Transaminase Activity ◽  
Specific Approach ◽  
Normal Tissues ◽  
The Past ◽  
Glycolytic Activity ◽  
Enzyme Characteristic ◽  
Phosphatase Alkaline

THE MEASUREMENT of enzyme activity of serum as an indicator of disease has a long history in medicine. In the past, it has been the aim of the designers of these methods to make them as specific as possible for assay of an enzyme characteristic of a particular system or group of similar organs. Examples of these venerable tests are those for amylase, acid phosphatase, alkaline phosphatase and choline esterase in the serum. Warburg made the first departure from this specificity by demonstrating that the activity of triosephosphate dehydrogenase in the serum of animals with cancer was much greater than that of controls. This test was partially specific, for as Warburg had earlier shown, the glycolytic activity of tumors is much greater than that of normal tissues. The non-specific approach became extreme with the introduction of the measurement of the glutamic-oxalacetic transaminase reaction in the diagnosis of acute coronary disease.

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

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.

Histochemical localization of phosphomonoesterases in Avhellina lahorea Woodland, 1927 (Cestoda: Anoplocephalida)

1984 ◽  
Vol 58 (2) ◽  
pp. 169-173 ◽  
Author(s):  
Rashid Farooq ◽  
H.U. Farooqi
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Adenosine Triphosphatase ◽  
Intestinal Parasite ◽  
Histochemical Localization ◽  
Sheep And Goats ◽  
Almost All ◽  
Phosphatase Alkaline

AbstractNon-specific and specific phosphatases have been histochemically localized in the tissues of Avitellina lahorea, an intestinal parasite of sheep and goats. Large quantities of acid phosphatase, alkaline phosphatase and adenosine triphosphatase were observed in almost all organs except the parenchyma where there were moderate amounts of acid phosphatase and no alkaline phosphatase; the reproductive ducts contained moderate amounts of alkaline phosphatase. 5-nucleotidase was observed only in the uterus, egg pouches and eggs and glucose-6-phosphatase activity was restricted to the tegument. The probable functions of these moieties at different sites are discussed.

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.

MORPHOLOGICAL AND GENETIC DIFFERENTIATION IN APHIDS (APHIDIDAE)

1981 ◽  
Vol 113 (6) ◽  
pp. 539-550 ◽  
Author(s):  
S. M. Singh ◽  
T. K. Cunningham
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Developmental Stages ◽  
Morphological Features ◽  
Malic Dehydrogenase ◽  
Enzyme Pattern ◽  
Parthenogenetic Reproduction ◽  
Host Plant Specificity ◽  
Leucine Alanine Peptidase ◽  
Phosphatase Alkaline

AbstractSix species of aphids belonging to four genera were measured for 12 morphological features at five developmental stages. It was concluded that reliable identification of species based on morphological features is possible only at adult stages. Samples were also analyzed for seven enzymes by gel electrophoresis. There were no enzyme pattern differences among developmental stages in any species. Three enzymes, malic dehydrogenase, malic enzyme and tetrazolium oxidase, showed the same band pattern in all species. The other four, acid phosphatase, alkaline phosphatase, esterase and leucine-alanine peptidase, showed “diagnostic” patterns specific to a given species. All species are easily identifiable by their esterase pattern which could be confirmed by acid phosphatase, alkaline phosphatase, and leucine-alanine peptidase patterns. The enzyme pattern differences were used to establish a dendrogram of genetic relationship among species which was compared with a dendrogram of morphological similarities. The close genetic similarity among species suggests that significant adaptive differentiation leading to speciation may have occurred within the context of relatively few genie changes. This is compatible with speciation in aphids being due primarily to their obligate parthenogenetic reproduction, frequent bottlenecks (drastic reduction in number), and host plant specificity.

Quantitative changes in acid phosphatase, alkaline phosphatase and 5‘-nucleotidase activity in rat liver after experimentally induced cholestasis

2008 ◽  
Vol 10 (3) ◽  
pp. 158-166 ◽  
Author(s):  
Wilma M. Frederiks ◽  
Cornelis J. F. Noorden ◽  
Daniël C. Aronson ◽  
Frans Marx ◽  
Klazina S. Bosch ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Rat Liver ◽  
Nucleotidase Activity ◽  
Quantitative Changes ◽  
Phosphatase Alkaline ◽  
Experimentally Induced

scholarly journals Lymphocyte and Granulocyte Enzyme Activity in Patients with Down’s Syndrome

Blood ◽  
1967 ◽  
Vol 30 (5) ◽  
pp. 669-673 ◽  
Author(s):  
HENRY L. NADLER ◽  
PATRICIA L. MONTELEONE ◽  
TOHRU INOUYE ◽  
DAVID YI-YUNG HSIA
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Blood Cells ◽  
Polymorphonuclear Leukocytes ◽  
White Blood Cells ◽  
Down's Syndrome ◽  
Down’S Syndrome ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Phosphatase Alkaline

Abstract Patients with trisomic Down’s syndrome were found to have significant increases of acid phosphatase, alkaline phosphatase, and glucose-6-phosphate dehydrogenase in both lymphocytes and polymorphonuclear leukocytes separated from white blood cells by the procedure of Rabinowitz. The alteration in enzyme activities appears not to be directly related to genes located on the chromosome causing Down’s syndrome.

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