A fluorescence turn-on probe for human (bovine) serum albumin based on the hydrolysis of a dioxaborine group promoted by proteins

2017 ◽  
Vol 53 (48) ◽  
pp. 6432-6435 ◽  
Author(s):  
Qian Sun ◽  
Weisi Wang ◽  
Zhaoyang Chen ◽  
Yuhua Yao ◽  
Weibing Zhang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
High Selectivity ◽  
Biologically Relevant ◽  
Turn On ◽  
Fluorescence Turn On ◽  
Hydrolysis Of

A reaction-based florescence probe CBF for serum albumin (SA) was proposed by connecting a dioxaborine unit with environment-sensitive coumarin fluorophore. CBF exhibits high selectivity and sensitivity toward SA over other biologically relevant species and has potential of detecting SA in biosamples.

Real-time optical measurement of biologically relevant thermal damage in tissue-mimicking hydrogels containing bovine serum albumin

2010 ◽  
Vol 26 (5) ◽  
pp. 456-464 ◽  
Author(s):  
Sacha D. Nandlall ◽  
Heiko A. Schiffter ◽  
Sebastian Vonhoff ◽  
Miriam Bazán-Peregrino ◽  
Manish Arora ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Real Time ◽  
Bovine Serum ◽  
Thermal Damage ◽  
Optical Measurement ◽  
Biologically Relevant

Deciphering the positional impact of chlorine in a new series of berberine analogues towards the superb-selective “turn-on” hydrophobic signaling of bovine serum albumin at physiological pH

2020 ◽  
Vol 44 (5) ◽  
pp. 1761-1771 ◽  
Author(s):  
Gopal Chandra Jana ◽  
Sk Nayim ◽  
Nandan Kumar Sahoo ◽  
Somnath Das ◽  
Mt Nasima Aktara ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Selective Detection ◽  
Turn On

We report a new 9-O-benzyl substituted berberine analogue for the selective detection of BSA with a limit of detection value of 3.30 nM.

scholarly journals Effects of weak bases on the degradation of endogenous and exogenous proteins by rat yolk sacs

1980 ◽  
Vol 188 (3) ◽  
pp. 895-903 ◽  
Author(s):  
G Livesey ◽  
K E Williams ◽  
S E Knowles ◽  
F J Ballard
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Normal Values ◽  
Free Medium ◽  
Weak Base ◽  
Weak Bases ◽  
Endogenous Proteins ◽  
Hydrolysis Of

In rat yolk sacs incubated in vitro, the rates of degradation of endogenous [3H]leucine-labelled proteins and of pinocytically ingested 125I-labelled bovine serum albumin were both decreased in the presence of either ammonium, methylammonium or ethylammonium ions (0-20 mM) or much lower concentrations of chloroquine (0-500 microM). These effects were also accompanied by an inhibition of pinocytosis, as measured by the rate of uptake of 125I-labelled polyvinylpyrrolidone, and by a fall in the [ATP]/[ADP] ratio within the tissue. Re-incubation in inhibitor-free medium of yolk sacs previously exposed to a weak base restored pinocytic and proteolytic capacities, except for tissues exposed to chloroquine at concentrations above 0.1 mM (these appeared to be cytotoxic); an attendent rise in [ATP]/[ADP] ratios to near normal values was also observed. Weak bases, at concentrations that fully arrested the breakdown of 125I-labelled albumin, failed to inhibit by more than 45% the degradation of [3H]leucine-labelled endogenous proteins. Since 125I-labelled bovine serum albumin has been shown to be degraded entirely intralysosomally by yolk sacs, this suggests either that the hydrolysis of endogenous proteins is shared between lysosomes and some other site or that, unlike 125I-labelled albumin, some endogenous proteins can be degraded within lysosomes at abnormally high pH.

A novel potentiometric sensor based on urease/ bovine serum albumin-poly(3,4-ethylenedioxythiophene)/Pt for urea detection

2016 ◽  
Vol 71 (4) ◽  
pp. 277-282 ◽  
Author(s):  
Chien-Hsing Hsu ◽  
Ya-Wei Hsu ◽  
Yu-Ching Weng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
High Selectivity ◽  
Ph Value ◽  
Detection Sensitivity ◽  
Urea Solution ◽  
Pt Electrode ◽  
Amide Bonds ◽  
Order Of Magnitude

AbstractWe have presented a potentiometric urea sensor using an urease/bovine serum albumin (BSA)-poly(3,4-ethylenedioxythiophene)(PEDOT)/Pt electrode. A urea detection sensitivity of 15.2 mV/decade (order of magnitude) has been achieved. BSA trapped in the PEDOT matrix was employed to bond urease molecules on the surface of a BSA-PEDOT/Pt electrode via amide bonds formed between the carboxyl functional groups on the enzyme and the amines on the BSA. The effects of PEDOT thickness, pH value of the urea solution, urease concentration, and temperature on the urea detection sensitivity were also studied. The lifetime of the sensor was studied for a period of 10 weeks, and the average sensing degradation rate was about 9 % per week. This sensor displayed a high selectivity to urea over glucose, KCl, and NaCl.

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