Protection of Carrageenin Edema and Trypsin Hydrolysis of Bovine Serum Albumin by Naphthylthiosemicarbazides and their Cyclized Oxadiazoles

Pharmacology ◽  
1976 ◽  
Vol 14 (5) ◽  
pp. 390-396 ◽  
Author(s):  
V. Kishore ◽  
S. Kumar ◽  
N.K. Narain ◽  
S.S. Parma ◽  
V.I. Stenberg
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Trypsin Hydrolysis ◽  
Hydrolysis Of ◽  
Carrageenin Edema

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 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.

Influence of Amitrole Upon Protein Metabolism in Bean Plants

Weed Science ◽  
1968 ◽  
Vol 16 (2) ◽  
pp. 222-226 ◽  
Author(s):  
John C. Brown ◽  
Mason C. Carter
Keyword(s):  
Free Radical ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radical Formation ◽  
Bean Plants ◽  
Free Radical Formation ◽  
Synthesis Activity ◽  
Hydrolysis Of ◽  
Bean Protein

No effect was shown of 3-amino-l,2,4-triazole (amitrole) upon the incorporation of alanine or histidine into soluble protein in bean (Phaseolus vulgaris L.) hypocotyls grown in darkness. The metabolic derivative of amitrole, β-(3-amino-1,2,4-triazolyl-l-)α-ala-nine (hereinafter referred to as 3-ATAL), also had no effect upon histidine incorporation. Serine incorporation was increased 56% in the presence of amitrole, but this may result from a reduction of endogenous serine pools. No evidence indicates a general disruption of protein synthesis. Activity from amitrole-5-14C was readily incorporated into bean protein, but hydrolysis revealed no 3-ATAL. Most of the activity was recovered as amitrole. Amitrole in the presence of riboflavin and light attacked bovine serum albumin, probably by free radical formation. Hydrolysis of bovine serum albumin revealed mainly amitrole. Apparently, the entry of amitrole into bean protein is by free radical formation.

scholarly journals The hydrolysis of proteins by microwave energy

1991 ◽  
Vol 13 (3) ◽  
pp. 93-95 ◽  
Author(s):  
Sam A. Margolis ◽  
Lois Jassie ◽  
H. M. Kingston
Keyword(s):  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Acid Hydrolysis ◽  
Bovine Serum ◽  
Microwave Energy ◽  
Complete Hydrolysis ◽  
Hydrolysis Conditions ◽  
Hydrolysis Of

Microwave energy, at manually-adjusted, partial power settings has been used to hydrolyse bovine serum albumin at 125 °C. Hydrolysis was complete within 2 h, except for valine and isoleucine which were completely liberated within 4 h. The aminoacid destruction was less than that observed at similar hydrolysis conditions with other methods and complete hydrolysis was achieved more rapidly. These results provide a basis for automating the process of amino-acid hydrolysis.

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