Synthesis, characterization, interactions with DNA and bovine serum albumin (BSA), and antibacterial activity of cyclometalated iridium(III) complexes containing dithiocarbamate derivatives

2014 ◽  
Vol 67 (15) ◽  
pp. 2643-2660 ◽  
Author(s):  
Titas Mukherjee ◽  
Manjira Mukherjee ◽  
Buddhadeb Sen ◽  
Snehasis Banerjee ◽  
Geeta Hundal ◽  
...  
RSC Advances ◽  
2018 ◽  
Vol 8 (60) ◽  
pp. 34252-34258 ◽  
Author(s):  
Cláudio Lourenço ◽  
Thomas J. Macdonald ◽  
Asterios Gavriilidis ◽  
Elaine Allan ◽  
Alexander J. MacRobert ◽  
...  

In this work we demonstrate that our active surfaces still show antibacterial activity even with BSA at low light.


2020 ◽  
Vol 240 ◽  
pp. 122115 ◽  
Author(s):  
Anupama R. Prasad ◽  
Sabeel M. Basheer ◽  
Induja R. Gupta ◽  
K.K. Elyas ◽  
Abraham Joseph

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Shu-Hua Kuo ◽  
Chi-Sheng Chien ◽  
Chun-Chi Wang ◽  
Chi-Jen Shih

The emergence of drug-resistant pathogens and the abuse of antibiotics have posed dominant threats to society. In this study, we propose an antibacterial use of bovine serum albumin-capped gold nanoclusters (BSA-AuNCs) to address the issue. BSA-AuNCs have a great antibacterial activity against MRSA and VISA which is proved by time-killing curves (TKC). The possible antibacterial mechanisms of BSA-AuNCs against MRSA and VISA are confirmed by fluorescence image observation.


Author(s):  
G. D. Gagne ◽  
M. F. Miller

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.


1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.


1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.


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