scholarly journals Molecular divergence of locally grown pumpkin (Cucurbita maxima) cultivars through some isozyme tests

2012 ◽  
Vol 19 ◽  
pp. 89-93
Author(s):  
ME Haque ◽  
MA Islam ◽  
B Sikdar
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Genetic Polymorphism ◽  
Malate Dehydrogenase ◽  
Polymorphism Analysis ◽  
Cucurbita Maxima ◽  
Extraction Buffer ◽  
Locally Grown ◽  
Its Polymorphism ◽  
Phosphatase Alkaline

Context: Pumpkin (Cucurbita maxima) is highly polymorphic vegetable species and its polymorphism can be analyzed by isozyme molecular marker. Objective: To analyze genetic polymorphism among 10 locally grown pumpkin cultivars by isozyme. Materials and Methods: Fresh leaves of young plant of different cultivars were used for enzyme extraction. Enzyme extracts were prepared by homogenizing of 2 g sample of each cultivar. Prechilled mortar and pestle nestled in ice along with 1% polyvinylpyrrolidone and 2 ml of chilled extraction buffer were used prior to centrifuge. N-PAGE was conducted for different isozymes and stained the gels with specific chemicals for band development. Results: Five isozymes (peroxidase, esterase, acid phosphatase, alkaline phosphatase and malate dehydrogenase) were tested for genetic polymorphism analysis of pumpkin cultivars. Among them esterase, peroxidase and alkaline phosphatase showed polymorphism in different cultivars with 75-, 58.33- and 41.18% respectively. But acid phosphatase and malate dehydrogenase did not show any polymorphism. Esterase and peroxidase produced band quickly than others. Relative mobility of first band of esterase, peroxidase, acid phosphatase, alkaline phosphatase and malate deghdrogenase was 0.063, 0.045, 0.262, 0.07 and 0.093 respectively Conclusion: Out of five isozymes, effective polymorphism was found in esterase and peroxidase test DOI: http://dx.doi.org/10.3329/jbs.v19i0.13006 J. bio-sci. 19 89-93, 2011

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.

The Influence of Short Ether Anesthesia on Some Liver Enzyme Activities in the Rat

1973 ◽  
Vol 51 (8) ◽  
pp. 604-607 ◽  
Author(s):  
E. Katona
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Urate Oxidase ◽  
Arylsulfatase A ◽  
Ether Anesthesia ◽  
Arylsulfatase B ◽  
Thiamine Pyrophosphatase ◽  
Liver Homogenates

Rats were anesthetized by ether inhalation for 4–5 min and sacrificed 1–48 h after anesthesia. From their liver homogenates, the activities of nine enzymes were determined. Activities of urate oxidase and arylsulfatase-A did not change significantly but arylsulfatase-B was slightly decreased. Malate dehydrogenase, arylsulfatase-B, and thiamine pyrophosphatase reached their highest and "malic enzymes" their lowest activities at the same time, 5 h after anesthesia. Alkaline phosphatase first decreased, later increased. Acid phosphatase and glucose-6-phosphatase activities decreased following ether anesthesia. Thesechanges in the enzyme activities generally agree and partly explain previously reported effects of ether anesthesia observed in the serum.

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 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>.

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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