scholarly journals Synthesis and biochemical characterization of silver nanoparticles grafted chitosan (Chi-Ag-NPs): in vitro studies on antioxidant and antibacterial applications

2020 ◽  
Vol 2 (4) ◽  
Author(s):  
Pavan Kumar Dara ◽  
R. Mahadevan ◽  
P. A. Digita ◽  
S. Visnuvinayagam ◽  
Lekshmi R. G. Kumar ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Biochemical Characterization ◽  
In Vitro Studies ◽  
Ag Nps

Functional and Biochemical Characterization of Immunologically Derived Equine Platelet-Activating Factor

1985 ◽  
Vol 22 (4) ◽  
pp. 375-386 ◽  
Author(s):  
H. C. Wimberly ◽  
D. O. Slauson ◽  
N. R. Neilsen
Keyword(s):  
Functional Activity ◽  
Biochemical Characterization ◽  
Platelet Activating Factor ◽  
Biochemical Properties ◽  
Naturally Occurring ◽  
Rabbit Platelets ◽  
Rapid Reaction ◽  
Specific Challenge

Antigen-specific challenge of equine leukocytes induced the non-lytic release of a platelet-activating factor in vitro. The equine platelet-activating factor stimulated the release of serotonin from equine platelets in a dose-responsive manner, independent of the presence of cyclo-oxygenase pathway inhibitors such as indomethacin. Rabbit platelets were also responsive to equine platelet-activating factor. The release of equine platelet-activating factor was a rapid reaction with near maximal secretion taking place in 30 seconds. Addition of equine platelet-activating factor to washed equine platelets stimulated platelet aggregation which could not be inhibited by the presence of aspirin or indomethacin. Platelets preincubated with equine platelet-activating factor became specifically desensitized to equine platelet-activating factor while remaining responsive to other platelet stimuli such as collagen and epinephrine. The following biochemical properties of equine platelet-activating factor are identical to those properties of 1-0-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine (AGEPC): stability upon exposure to air and acid; loss of functional activity after basecatalyzed methanolysis with subsequent acylation that returned all functional activity; and identical relative mobilities on silica gel G plates developed with chloroform:methanol:water (65:35:6, volume/volume). The combined functional and biochemical characteristics of equine platelet-activating factor strongly suggest identity between this naturally occurring, immunologically derived equine factor and AGEPC.

scholarly journals Intermediate filaments in non-neuronal cells of invertebrates: isolation and biochemical characterization of intermediate filaments from the esophageal epithelium of the mollusc Helix pomatia.

1985 ◽  
Vol 101 (2) ◽  
pp. 427-440 ◽  
Author(s):  
E Bartnik ◽  
M Osborn ◽  
K Weber
Keyword(s):  
Positive Reaction ◽  
Intermediate Filaments ◽  
Biochemical Characterization ◽  
Helix Pomatia ◽  
Molar Ratio ◽  
Negative Stain ◽  
Epithelial Morphology ◽  
Lower Chordate

To screen invertebrate tissues for the possible expression of intermediate filaments (IFs), immunofluorescence microscopy with the monoclonal antibody anti-IFA known to detect all mammalian IF proteins was used (Pruss, R. M., R. Mirsky, M. C. Raff, R. Thorpe, A. J. Dowding, and B. H. Anderton. 1981. Cell, 27:419-428). In a limited survey, the lower chordate Branchiostoma as well as the invertebrates Arenicola, Lumbricus, Ascaris, and Helix pomatia revealed a positive reaction primarily on epithelia and on nerves, whereas certain other invertebrates appeared negative. To assess the nature of the positive reaction, Helix pomatia was used since a variety of epithelia was strongly stained by anti-IFA. Fixation-extraction procedures were developed that preserve in electron micrographs of esophagus impressive arrays of IFs as tonofilament bundles. Fractionation procedures performed on single cell preparations document large meshworks of long and curvilinear IF by negative stain. These structures can be purified. One- and two-dimensional gels show three components, all of which are recognized by anti-IFA in immunoblotting: 66 kD/pl 6.35, 53 kD/pl 6.05, and 52 kD/pl 5.95. The molar ratio between the larger and more basic polypeptide and the sum of the two more acidic forms is close to 1. After solubilization in 8.5 M urea, in vitro filament reconstitution is induced when urea is removed by dialysis against 2-50 mM Tris buffer at pH 7.8. The reconstituted filaments contain all three polypeptides. The results establish firmly the existence of invertebrate IFs outside neurones and demonstrate that the esophagus of Helix pomatia displays IFs which in line with the epithelial morphology of the tissue could be related to keratin IF of vertebrates.

In Vitro Biochemical Characterization of Cytokinesis Actin-Binding Proteins

2016 ◽  
pp. 151-179 ◽  
Author(s):  
Dennis Zimmermann ◽  
Alisha N. Morganthaler ◽  
David R. Kovar ◽  
Cristian Suarez
Keyword(s):  
Binding Proteins ◽  
Biochemical Characterization ◽  
Actin Binding ◽  
Actin Binding Proteins

Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase II in vitro

FEBS Letters ◽  
1998 ◽  
Vol 428 (3) ◽  
pp. 235-240 ◽  
Author(s):  
Kenzo Ohtsuki ◽  
Toshiro Maekawa ◽  
Shigeyoshi Harada ◽  
Atsushi Karino ◽  
Yuko Morikawa ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Hiv 1

Silver nanoparticles used to counter Monilinia fructicola fungicide-resistance and reduce fungicide environmental footprint 

2021 ◽  
Author(s):  
Constantinos Chrysikopoulos ◽  
Anastasios A. Malandrakis ◽  
Nektarios Kavroulakis ◽  
Anthi Stefanarou
Keyword(s):  
Silver Nanoparticles ◽  
Control Plant ◽  
Resistance Mutation ◽  
Silver Ions ◽  
Apple Fruit ◽  
Ag Nps ◽  
Gene Target ◽  
Benzimidazole Fungicides

<div><span>The potential of silver nanoparticles (Ag-NPs) to control plant pathogen <em>Monilia</em><em>fructicola </em>and to deter environmental contamination by reducing fungicide doses was evaluated <em>in vitro </em>and <em>in vivo. </em> </span>F<span>ungitoxicity screening </span>of <em><span>M. fructicola </span></em><span>isolates resulted in the detection of 18 benzimidazole-resistant (BEN-R) isolates with reduced sensitivity to fungicides  thiophanate methyl (TM)  and carbendazim. All resistant isolates caried the E198A resistance mutation in their </span><em><span>β</span>-</em>tubulin gene, target site of the benzimidazole fungicides. <span>Ag-NPs could effectively control both sensitive (BEN-S) and resistant isolates while the combination of Ag-NPs with TM significantly enhanced their fungitoxic effect both <em>in vitro </em>and in apple fruit tests. The positive correlation observed between Ag-NPs and TM+Ag-NPs treatments indicates a mixture-enhanced Ag-NPs activity/availability as a possible mechanism of synergy. No correlation between Ag-NPs  and AgNO<sub>3 </sub>could  be found suggesting difference(s) in the fungitoxic mechanism of action between Nps and their bulk/ionic counterparts. Indications of the involvement of energy (ATP) metabolism in the mode of action of Ag-NPs were also evident by the synergy observed between Ag-NPs and the </span>oxidative phosphorylation<span>-uncoupler fluazinam (FM) against both BEN-R and BEN-S phenotypes. The role of silver ions release on the inhibitory action of Ag-NPs against the fungusis probably limited since the AgNPs/NaCl combination enhanced fungitoxicity, a fact that could not be justified by the expected binding of silver with chlorine ions. Concluding, Ag-NPs can be effectively used as a means of controlling both BEN-S and BEN-R <em>M. </em><em>fructicola </em>isolates </span>while <span>their combination with conventional fungicides should aid anti-resistant strategies and reduce the environmental impact of synthetic fungicides by reducing effective doses to the control the pathogen.</span></div>

scholarly journals Identification and characterization of cytochrome P450 1232A24 and 1232F1 from Arthrobacter sp. and their role in the metabolic pathway of papaverine

2019 ◽  
Vol 166 (1) ◽  
pp. 51-66 ◽  
Author(s):  
Jan M Klenk ◽  
Max-Philipp Fischer ◽  
Paulina Dubiel ◽  
Mahima Sharma ◽  
Benjamin Rowlinson ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Metabolic Pathway ◽  
Biochemical Characterization ◽  
Gene Clusters ◽  
Cytochrome P450 Monooxygenases ◽  
Dihydroxyphenylacetic Acid ◽  
Meta Position ◽  
Redox Partners

AbstractCytochrome P450 monooxygenases (P450s) play crucial roles in the cell metabolism and provide an unsurpassed diversity of catalysed reactions. Here, we report the identification and biochemical characterization of two P450s from Arthrobacter sp., a Gram-positive organism known to degrade the opium alkaloid papaverine. Combining phylogenetic and genomic analysis suggested physiological roles for P450s in metabolism and revealed potential gene clusters with redox partners facilitating the reconstitution of the P450 activities in vitro. CYP1232F1 catalyses the para demethylation of 3,4-dimethoxyphenylacetic acid to homovanillic acid while CYP1232A24 continues demethylation to 3,4-dihydroxyphenylacetic acid. Interestingly, the latter enzyme is also able to perform both demethylation steps with preference for the meta position. The crystal structure of CYP1232A24, which shares only 29% identity to previous published structures of P450s helped to rationalize the preferred demethylation specificity for the meta position and also the broader substrate specificity profile. In addition to the detailed characterization of the two P450s using their physiological redox partners, we report the construction of a highly active whole-cell Escherichia coli biocatalyst expressing CYP1232A24, which formed up to 1.77 g l−1 3,4-dihydroxyphenylacetic acid. Our results revealed the P450s’ role in the metabolic pathway of papaverine enabling further investigation and application of these biocatalysts.

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