scholarly journals Denitrifying Activity and Homologous Enzyme Analysis of Alcanivorax dieselolei Strain N1203

2009 ◽  
Vol 14 (3) ◽  
pp. 97-105 ◽  
Author(s):  
MIYO NAKANO ◽  
SUGURU OKUNISHI ◽  
REIJI TANAKA ◽  
HIROTO MAEDA
Keyword(s):  
Enzyme Analysis ◽  
Homologous Enzyme

Evaluation of Azadirachtin on Arthrospira plantensis Gomont growth parameters and antioxidant enzymes

2020 ◽  
Vol 56 ◽  
pp. 8
Author(s):  
Hatice Tunca ◽  
Ali Doğru ◽  
Feray Köçkar ◽  
Burçin Önem ◽  
Tuğba Ongun Sevindik
Keyword(s):  
Enzyme Activity ◽  
Growth Parameters ◽  
Arthrospira Platensis ◽  
Proline Content ◽  
Enzyme Analysis ◽  
Free Proline ◽  
Sod Activity ◽  
Pesticide Pollution ◽  
Antioxidant Parameters ◽  
Mda Content

Azadirachtin (Aza) used as insecticide due to inhibiting growth of insects and preventing them from feeding on plants. To understand the effects of contamination of this insecticide on phototrophs, and to determine the responses of these organisms against these insecticides are extremely important in understanding how the ecosystem is affected. In this study, chlorophyll-a amount, OD 560 and antioxidant parameters (total SOD, APX, GR, Proline, MDA and H2O2) were determined in order to understand the effect of Aza on Arthrospira platensis Gomont. Aza was applied between 0–20 μg mL−1 concentrations for 7 days in the study. Enzyme analysis was conducted at the end of the 7th day. There was a statistically significant decrease in the absorbance of OD560 and the chlorophyll-a content in A. platensis cultures exposed to the Aza (0–20 μg mL−1) during 7 days due to the increase in pesticide levels. SOD activity decreased at 8, 16 and 20 μg mL−1 concentrations; GR enzyme activity showed a significant decrease compared to the control at a concentration of 20 μg mL−1. APX activity did not change significantly compared to control. The MDA content increased significantly at 16 and 20 μg mL−1 concentrations. The H2O2 content significantly increased at 12, 16 and 20 μg mL−1 concentrations (p < 0.05) while the free proline content decreased at 4 μg mL−1 concentration (p < 0.05). As a result, regarding the Aza concentrations used in this study may be a step to prevent pesticide pollution in the environment.

IMMUNE STATUS OF EPSTEIN - BARR VIRUS-INFECTED CHILDREN WITH SECRETORY MIDDLE OTITIS

2020 ◽  
pp. 60-64
Author(s):  
Alina Volodymyrivna Chumakova ◽  
Yuliia Viktorivna Lozova
Keyword(s):  
Otitis Media ◽  
Epstein Barr Virus ◽  
Immune Status ◽  
Enzyme Analysis ◽  
Comprehensive Treatment ◽  
Upper Respiratory Tract ◽  
Adequate Treatment ◽  
Barr Virus ◽  
Cell Immunity ◽  
Epstein Barr

Recently the role of herpes viruses in an aggravation of inflammatory diseases of the upper respiratory tract, in particular, herpes simplex virus and Epstein − Barr virus, has become increasingly evident in otorhynolaryngology practice. To determine the extent of infection with Epstein − Barr virus and to study the immunogram of the first level for the children with secretory otitis media, 48 patients aged 3−9 years were examined for the purpose of an adequate treatment. Infection was revealed by serological diagnosis (enzyme immunoassay) with the determination of IgM to capsid complex (VCA) and IgG to early antigen (EA). Level 1 immunograms were also determined by immune enzyme analysis. Children with secretive middle otitis (22.9 %) were infected with Epstein − Barr virus, corresponding to an acute phase of the disease, as well as they had a reduce cell immunity. All children received comprehensive treatment for secretory middle otitis. It was concluded about the need for children with middle otitis to be screened for an infection with the Epstein−Barr virus and treated conservatively by an immunologist. Key words: secretory middle otitis media, etiology of Epstein − Barr virus, immune status of children, treatment.

Central and peripheral adaptations of the gas transport system to one-leg training

1981 ◽  
Vol 59 (11) ◽  
pp. 1146-1154 ◽  
Author(s):  
S. G. Thomas ◽  
D. A. Cunningham ◽  
M. J. Plyley ◽  
D. R. Boughner ◽  
R. A. Cook
Keyword(s):  
Cardiac Output ◽  
Oxygen Uptake ◽  
Endurance Training ◽  
Maximal Oxygen Uptake ◽  
Enzyme Activities ◽  
Cardiovascular Responses ◽  
Cycle Ergometer ◽  
Left Ventricular ◽  
Enzyme Analysis ◽  
Ergometer Exercise

The role of central and peripheral adaptations in the response to endurance training was examined. Changes in cardiac structure and function, oxygen extraction, and muscle enzyme activities following one-leg training were studied.Eleven subjects (eight females, three males) trained on a cycle ergometer 4 weeks with one leg (leg 1), then 4 weeks with the second leg (leg 2). Cardiovascular responses to exercise with both legs and each leg separately were evaluated at entry (T1), after 4 weeks of training (T2), and after a second 4 weeks of training (T3). Peak oxygen uptake ([Formula: see text] peak) during exercise with leg 1 (T1 to T2 increased 19.8% (P < 0.05) and during exercise with leg 2 (T2 to T3 increased 16.9% (P < 0.05). Maximal oxygen uptake with both legs increased 7.9% from T1 to T2 and 9.4% from T2 to T3 (P < 0.05). During exercise at 60% of [Formula: see text] peak, cardiac output [Formula: see text] was increased significantly only when the trained leg was exercised. [Formula: see text] increased 12.2% for leg 1 between T1 and T2 and 13.0% for leg 2 between T2 and T3 (P < 0.05). M-mode echocardiographic assessment of left ventricular internal diameter at diastole and peak velocity of circumferential fibre shortening at rest or during supine cycle ergometer exercise at T1 and T3 revealed no training induced changes in cardiac dimensions or function. Enzyme analysis of muscle biopsy samples from the vastus lateralis (At T1, T2, T3) revealed no consistent pattern of change in aerobic (malate dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase) or anaerobic (phosphofructokinase, lactate dehydroginase, and creatine kinase) enzyme activities. Increases in cardiac output and maximal oxygen uptake which result from short duration endurance training can be achieved, therefore, without measurable central cardiac adaptation. The absence of echocardio-graphically determined changes in cardiac dimensions and contractility and the absence of an increase in cardiac output during exercise with the nontrained leg following training of the contralateral limb support this conclusion.

Enzyme analysis of Atheris snake venom

Toxicon ◽  
1997 ◽  
Vol 35 (6) ◽  
pp. 813 ◽  
Author(s):  
D. Mebs ◽  
A. Fach ◽  
H.-W. Herrmann
Keyword(s):  
Snake Venom ◽  
Enzyme Analysis

scholarly journals Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50

1979 ◽  
Vol 179 (2) ◽  
pp. 333-339 ◽  
Author(s):  
A Y Strongin ◽  
D I Gorodetsky ◽  
I A Kuznetsova ◽  
V V Yanonis ◽  
Z T Abramov ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Serine Proteinase ◽  
Subtilis Strain ◽  
Bacterial Strains ◽  
Terminal Sequence ◽  
Gramicidin S ◽  
Intracellular Enzymes ◽  
Sepharose 4B ◽  
Homologous Enzyme ◽  
Strict Selection

Intracellular serine proteinase was isolated from sporulating cells of Bacillus subtilis Marburg 168 by gramicidin S-Sepharose 4B affinity chromatography. The enzymological characteristics, the amino acid composition and the 19 residues of the N-terminal sequence of the enzyme are reported. The isolated proteinase was closely related to, but not completely identical with, the intracellular serine proteinase of B. subtilis A-50. The divergence between these two intracellular enzymes was less than that between the corresponding extracellular serine proteinases (subtilisins) of types Carlsberg and BPN′!, produced by these bacterial strains. This may be connected with the more strict selection constraints imposed in intracellular enzymes during evolution.

scholarly journals A molecular characterization ofClostridium difficileisolates from humans, animals and their environments

1993 ◽  
Vol 111 (2) ◽  
pp. 257-264 ◽  
Author(s):  
G. O'Neill ◽  
J. E. Adams ◽  
R. A. Bowman ◽  
T. V. Riley
Keyword(s):  
Fragment Length Polymorphism ◽  
Hospital Environment ◽  
Enzyme Analysis ◽  
Restriction Enzyme Analysis ◽  
Direct Transmission ◽  
Chromosomal Dna ◽  
Veterinary Clinic ◽  
Enhanced Chemiluminescence ◽  
Typing Methods ◽  
Rflp Typing

SummaryIt is generally accepted that most patients withClostridium difficile-associated diarrhoea acquire the organism from the environment. Recently we demonstrated that household pets may constitute a significant reservoir ofC. difficilethrough gastrointestinal carriage in up to 39% of cats and dogs. These findings suggested that direct transmission from household pets, or contamination of the environment by them, may be a factor in the pathogenesis ofC. difficile-associated diarrhoea. To investigate this possibility, we examined isolates ofC. difficilefrom humans, pets and the environment by restriction enzyme analysis (REA) and restriction fragment length polymorphism (RFLP) typing using enhanced chemiluminescence. Both REA and RFLP typing methods usedHindIII digests of chromosomal DNA. A total of 116 isolates ofC. difficilefrom pets (26), veterinary clinic environmental sites (33), humans (37) and hospital environmental sites (20) was examined. REA was far more discriminatory than RFLP typing and for all isolates there were 34 REA types versus 6 RFLP types. There was good correlation between the REA types found in isolates from pets and from the veterinary clinic environment, and between isolates from humans and from those found in the hospital environment. There was, however, no correlation between REA type ofC. difficilefound in pets and isolates of human origin. We conclude that there may still be a risk of humans acquiringC. difficilefrom domestic pets as these findings may be the result of geographical variation.

scholarly journals Specific Detection of Xanthomonas axonopodis pv. dieffenbachiae in Anthurium (Anthurium andreanum) Tissues by Nested PCR

2006 ◽  
Vol 72 (2) ◽  
pp. 1072-1078 ◽  
Author(s):  
Isabelle Robène-Soustrade ◽  
Philippe Laurent ◽  
Lionel Gagnevin ◽  
Emmanuel Jouen ◽  
Olivier Pruvost
Keyword(s):  
Diagnostic Tool ◽  
Nested Pcr ◽  
Restriction Analysis ◽  
Detection Threshold ◽  
Enzyme Analysis ◽  
Restriction Enzyme Analysis ◽  
Amplification Product ◽  
Xanthomonas Axonopodis ◽  
Sequence Characterized Amplified Region ◽  
Pcr Test

ABSTRACT Efficient control of Xanthomonas axonopodis pv. dieffenbachiae, the causal agent of anthurium bacterial blight, requires a sensitive and reliable diagnostic tool. A nested PCR test was developed from a sequence-characterized amplified region marker identified by randomly amplified polymorphic DNA PCR for the detection of X. axonopodis pv. dieffenbachiae. Serological and pathogenicity tests were performed concurrently with the nested PCR test with a large collection of X. axonopodis pv. dieffenbachiae strains that were isolated worldwide and are pathogenic to anthurium and/or other aroids. The internal primer pair directed amplification of the expected product (785 bp) for all 70 X. axonopodis pv. dieffenbachiae strains pathogenic to anthurium tested and for isolates originating from syngonium and not pathogenic to anthurium. This finding is consistent with previous studies which indicated that there is a high level of relatedness between strains from anthurium and strains from syngonium. Strains originating from the two host genera can be distinguished by restriction analysis of the amplification product. No amplification product was obtained with 98 strains of unrelated phytopathogenic bacteria or saprophytic bacteria from the anthurium phyllosphere, except for a weak signal obtained for one X. axonopodis pv. allii strain. Nevertheless, restriction enzyme analysis permitted the two pathovars to be distinguished. The detection threshold obtained with pure cultures or plant extracts (103 CFU ml−1) allowed detection of the pathogen from symptomless contaminated plants. This test could be a useful diagnostic tool for screening propagation stock plant material and for monitoring international movement of X. axonopodis pv. dieffenbachiae.

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