Geothermal Effects on Multiple Enzyme Forms in the Lichen Cladonia Mitis

1992 ◽  
Vol 24 (2) ◽  
pp. 181-192
Author(s):  
Dianne Fahselt
Keyword(s):  
Alkaline Phosphatase ◽  
Superoxide Dismutase ◽  
Glutamate Dehydrogenase ◽  
Isoelectric Focusing ◽  
Similarity Coefficient ◽  
Close Proximity ◽  
Neighbouring Area ◽  
Complementary Techniques ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Polymorphic Enzymes

Abstract Samples of Cladonia mitis were collected from three microhabitats within an open field in eastern Hokkaido, Japan. Two sets of sample thalli were taken in close proximity to geothermal vents and a third from a neighbouring area not directly affected by outgassings. Enzymes were extracted and separated by isoelectric focusing, and multiple enzyme forms of three oxidoreductases, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase and superoxide dismutase, and two hydrolases, esterase and alkaline phosphatase, were examined. Similarities between microhabitats based on electrophoretic results were calculated using Jaccard's similarity coefficient and expressed graphically through the complementary techniques of clustering and ordination. All of the major differences in isozyme patterns between remote samples and those near fumaroles were in the two highly polymorphic enzymes, esterase and alkaline phosphatase. Differences were as great or greater than those between geographically separated conspecific populations of lichens examined previously. In the more sulphurous microhabitats, nine bands were much more frequent and eight much less so than in locations further from the source of gases.

Constancy of enzyme electrofocusing patterns in a stand of the lichen Umbilicaria mammulata

1986 ◽  
Vol 64 (9) ◽  
pp. 1928-1934 ◽  
Author(s):  
C. Hageman ◽  
D. Fahselt
Keyword(s):  
Alkaline Phosphatase ◽  
Superoxide Dismutase ◽  
Glutamate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Mannitol Dehydrogenase ◽  
Specific Staining ◽  
Phosphogluconate Dehydrogenase ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Sampling Times ◽  
Umbilicaria Mammulata

Thalli of the lichen Umbilicaria mammulata (Ach.) Tuck, were collected from one site, 24 at each of five different sampling times, over a period of 1 year. Protein extracts from each individual thallus were subjected to isoelectric focusing, followed by specific staining for eight enzyme systems (mannitol dehydrogenase, isocitrate dehydrogenase, 6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, superoxide dismutase, esterase, and alkaline phosphatase). A total of 55 bands were resolved, 25 of which were constant in all thalli through all sampling dates. Principal components analysis of the electromorph data showed the existence of groups corresponding to sets of thalli collected at the same times; esterase and alkaline phosphatase variation were primarily responsible for these groupings. Banding patterns of 6-phosphogluconate dehydrogenase and superoxide dismutase were constant regardless of date of collection. Most bands of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were consistent through all sampling times, but each system exhibited one band that differed in frequency from one collection date to another. Electromorphs of mannitol dehydrogenase and isocitrate dehydrogenase exhibited only minor variability. Dehydrogenase enzymes, since they tended to vary least from one sampling time to the next, can thus be used more readily for taxonomic purposes. If esterases and alkaline phosphatases are to be applied as taxonomic criteria, samples for comparison should be collected simultaneously.

Measurement of Intrapopulational Enzyme Variation in Five Species of Epiphytic Lichens

1988 ◽  
Vol 20 (4) ◽  
pp. 377-384 ◽  
Author(s):  
Dianne Fahselt
Keyword(s):  
Alkaline Phosphatase ◽  
Superoxide Dismutase ◽  
Sexual Reproduction ◽  
Isoelectric Focusing ◽  
Evolutionary History ◽  
Enzyme System ◽  
Epiphytic Lichens ◽  
Enzyme Variation ◽  
Enzyme Systems ◽  
Individual Bands

AbstractThalli of five species of epiphytic lichens were collected from one moribund spruce-fir stand in the Algonquin Highlands in Ontario, Canada. Extracts of all were subjected to isoelectric focusing and stained for activity of 16 enzyme systems. Gels were scored for the presence or absence of individual bands in each enzyme system, and the degree of polymorphism of all detectable enzymes was evaluated using a variability measure developed for use with presence/absence data. Esterase and alkaline phosphatase showed the greatest amount of polymorphism and superoxide dismutase was the least variable enzyme system. The degree of enzyme variability in each of the five species was probably a reflection of its past evolutionary history and bore little relationship to apparent potential for sexual reproduction.

STUDY OF THE COMBINED INFLUENCE OF SODIUM THIOPENTAL AND DELTA SLEEP-INDUCING PEPTIDE ON ANTIOXIDANT DEFENSE SYSTEM IN RATS

2016 ◽  
pp. 49-52
Author(s):  
A. V. Shvetsov ◽  
E. G. Batotsyrenova ◽  
N. A. Dyuzhikova ◽  
V. A. Kashuro ◽  
N. V. Lapina ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Defense ◽  
Antioxidant Defense System ◽  
Time Interval ◽  
Sodium Thiopental ◽  
Antioxidant Defense Enzymes ◽  
Delta Sleep ◽  
Thiopental Coma ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Delta Sleep Inducing Peptide

A biochemical investigation was performed into activity of rat antioxidant defense enzymes at different time interval after administration of sodium thiopental and delta-sleep-inducing peptide (DSIP). It was shown that thiopental coma was accompanied by a decreased level of superoxide dismutase ( 6 and 24 h after exposure) and increased level of caspase-3 ( 6 h after exposure) in the rat blood plasma. A pharmacological correction with DSIP induced a decrease of the level of superoxide dismutase ( 6 and 24 h after exposure), glutathione peroxidase and glucose 6-phosphate dehydrogenase (after 6h).

Catalase released from beneficial and plant-pathogenic pseudomonads by water and chloroform treatments

1994 ◽  
Vol 40 (8) ◽  
pp. 630-636
Author(s):  
J. I. Pounder ◽  
A. J. Anderson
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Water Treatment ◽  
Pseudomonas Syringae ◽  
Small Proportion ◽  
Plant Colonization ◽  
Periplasmic Proteins ◽  
Specific Activities ◽  
Leaf Pathogen ◽  
Glucose 6 Phosphate Dehydrogenase

Survival of pseudomonads during plant colonization may involve bacterial catalases to degrade the hydrogen peroxide produced by the plant. The specific activities of catalases in lysates from two saprophytic isolates of Pseudomonas putida and Pseudomonas fluorescens and three races of Pseudomonas syringae pv. glycinea were similar. To explore the location of the bacterial catalases, cells of the pathogenic and saprophytic pseudomonads were treated with chloroform, which is reported to release periplasmic proteins. Although catalase was released by chloroform treatment, the cytoplasmic enzymes isocitrate dehydrogenase, superoxide dismutase, and glucose-6-phosphate dehydrogenase were also detected. These proteins may have come from lysis of a small proportion of the cells rather than the periplasm. Water treatment of cells also released amounts of protein similar to those derived from chloroform treatment. Similar responses were found from both pathogenic and saprophytic strains. The release of catalase and proteins from the leaf pathogen P. syringae pv. glycinea race 0 and the root-associated saprophyte P. putida decreased as the cultures aged. With P. putida and P. syringae pv. glycinea race 0, the single isozyme of catalase released by water and chloroform treatment also was detected in lysates. Additional catalase isozymes were present in lysates as the cultures aged.Key words: periplasmic proteins, survival.

Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing

1997 ◽  
Vol 71 (2) ◽  
pp. 175-181 ◽  
Author(s):  
M. Sène ◽  
P. Brémond ◽  
J.P. Hervé ◽  
V.R. Southgate ◽  
B. Sellin ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Schistosoma Mansoni ◽  
Isoelectric Focusing ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Arvicanthis Niloticus

AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

scholarly journals Evidence for the importance of arginine residues in pig kidney alkaline phosphatase

1979 ◽  
Vol 181 (1) ◽  
pp. 137-142 ◽  
Author(s):  
M N Woodroofe ◽  
P J Butterworth
Keyword(s):  
Alkaline Phosphatase ◽  
Active Site ◽  
Competitive Inhibitor ◽  
Arginine Residue ◽  
Pig Kidney ◽  
Close Proximity ◽  
Arginine Residues ◽  
Km Value ◽  
Uncompetitive Inhibitor ◽  
Kidney Alkaline Phosphatase

The arginine-specific reagents 2,3-butanedione and phenylglyoxal inactivate pig kidney alkaline phosphatase. As inactivation proceeds there is a progressive fall in Vmax. of the enzyme, but no demonstrable change in the Km value for substrate. Pi, a competitive inhibitor, and AMP, a substrate of the enzyme, protect alkaline phosphatase against the arginine-specific reagents. These effects are explicable by the assumption that the enzyme contains an essential arginine residue at the active site. Protection is also afforded by the uncompetitive inhibitor NADH through a partially competive action against the reagents. Enzyme that has been exposed to the reagents has a decreased sensitivity to NADH inhibition. It is suggested that an arginine residue is important for NADH binding also, although this residue is distinct from that at the catalytic site. The protection given by NADH against loss of activity is indicative of the close proximity of the active and NADH sites.

Protective Effects of Ginsenosides on 17α-Ethynyelstradiol-Induced Intrahepatic Cholestasis via Anti-Oxidative and Anti-Inflammatory Mechanisms in Rats

2017 ◽  
Vol 45 (08) ◽  
pp. 1613-1629 ◽  
Author(s):  
Yan-Jiao Xu ◽  
Zao-Qin Yu ◽  
Cheng-Liang Zhang ◽  
Xi-Ping Li ◽  
Cheng-Yang Feng ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Alkaline Phosphatase ◽  
Superoxide Dismutase ◽  
Protein Expression ◽  
Intrahepatic Cholestasis ◽  
Serum Levels ◽  
Total Bile Acid ◽  
Protective Effects ◽  
Sod Activity ◽  
Mda Content

The present study was designed to assess the effects and potential mechanisms of ginsenosides on 17[Formula: see text]-ethynyelstradiol (EE)-induced intrahepatic cholestasis (IC). Ginsenoside at doses of 30, 100, 300[Formula: see text]mg/kg body weight was intragastrically (i.g.) given to rats for 5 days to examine the effect on EE-induced IC. Serum levels of alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), and total bile acid (TBA) were measured. Hepatic malondialdehyde (MDA) content and superoxide dismutase (SOD) activity were determined. Protein expression of proinflammatory cytokines TNF-[Formula: see text], IL-6 and IL-1[Formula: see text] was analyzed by immunohistochemistry and Western blot. Results indicated that ginsenosides remarkably prevented EE-induced increase in the serum levels of AST, ALT, ALP and TBA. Moreover, the elevation of hepatic MDA content induced by EE was significantly reduced, while hepatic SOD activities were significantly increased when treated with ginsenosides. Histopathology of the liver tissue showed that pathological injuries were relieved after treatment with ginsenosides. In addition, treatment with ginsenosides could significantly downregulate the protein expression of TNF-[Formula: see text], IL-6 and IL-1[Formula: see text] compared with EE group. These findings indicate that ginsenosides exert the hepatoprotective effect on EE-induced intrahepatic cholestasis in rats, and this protection might be attributed to the attenuation of oxidative stress and inflammation.

Cytokines increase rat lung antioxidant enzymes during exposure to hyperoxia

1989 ◽  
Vol 66 (2) ◽  
pp. 1003-1007 ◽  
Author(s):  
C. W. White ◽  
P. Ghezzi ◽  
S. McMahon ◽  
C. A. Dinarello ◽  
J. E. Repine
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Antioxidant Enzyme ◽  
Enzyme Activities ◽  
Tumor Necrosis ◽  
Interleukin 1 ◽  
Antioxidant Enzyme Activities ◽  
Rat Lung ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Necrosis Factor

Pretreatment with the combination of tumor necrosis factor/cachectin (TNF/C) and interleukin 1 (IL-1) increased glucose-6-phosphate dehydrogenase (G6PDH), glutathione reductase (GR), glutathione peroxidase (GPX), catalase (CAT), and superoxide dismutase (SOD) activities in lungs of rats continuously exposed to hyperoxia for 72 h, a time when all untreated rats had already died. Pretreatment with TNF/C and IL-1 also increased, albeit slightly, lung G6PDH and GR activities of rats exposed to hyperoxia for 4 or 16 h. By comparison, no differences occurred in lung antioxidant enzyme activities of TNF/C and IL-1- or saline-pretreated rats exposed to hyperoxia for 36 or 52 h; the latter is a time just before untreated rats began to succumb during exposure to hyperoxia. The results raise the possibility that TNF/C and IL-1 treatment can increase lung antioxidant enzyme activities and that increased lung antioxidant enzymes may contribute to the increased survival of TNF/C and IL-1-pretreated rats in hyperoxia for greater than 72 h.

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