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.

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.

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.

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 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>.

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.

Sign in / Sign up

Export Citation Format

Share Document