Thermal hazards and kinetic analysis of salicyl hydroxamic acid under isothermal and adiabatic conditions

2016 ◽  
Vol 623 ◽  
pp. 43-49 ◽  
Author(s):  
Gui-bin Lu ◽  
Cai-xing Zhang ◽  
Wang-hua Chen ◽  
Li-ping Chen ◽  
Yi-shan Zhou
JOM ◽  
2018 ◽  
Vol 70 (12) ◽  
pp. 2813-2818 ◽  
Author(s):  
Wei Yao ◽  
Maolin Li ◽  
Rui Cui ◽  
Xingke Jiang ◽  
Hongqiang Jiang ◽  
...  

1981 ◽  
Vol 37 (12) ◽  
pp. 1290-1291 ◽  
Author(s):  
A. J. Barnicoat ◽  
W. G. van't Hoff ◽  
P. J. Morrison ◽  
H. J. Rogers

Genetics ◽  
1979 ◽  
Vol 93 (3) ◽  
pp. 539-555
Author(s):  
Thad H Pittenger ◽  
David J West

ABSTRACT Filtration-enrichment and inositol-less death methods of mutant isolation, coupled with a screen for cyanide-insensitive respiration, proved to be highly efficient methods for isolating temperature-sensitive (ts) nuclear Neurospora mutants having defective respiration. Eighteen different ts respiratory mutants have been isolated. Most of them are pleiotropic and defective in one or more of the following phenotypes: cytochrome aa3, b, and c (individual or multiple defects); oligomycin inhibition of ATPase activity; respiration and its inhibition by KCN and salicyl hydroxamic acid; and growth rates in liquid and solid media at 25° and 38°. Among these mutants are the first cytochrome c mutant of Neurospora and an extranuclear ts ATPase mutant. An added bonus was the fact that aver half of the mutants were affected either in ribosome assembly or in protein synthesis in the mitochondrion. We have yet to find any mutants completely lacking activities associated with the respiratory chain. However, the wide spectrum of mutants isolated here, along with those currently available, constitutes a considerable resource for investigating respiration in obligate aerobes.


2013 ◽  
Vol 52 (1-2) ◽  
pp. 139-147 ◽  
Author(s):  
Janusz Czapski

Latent form of mushroom catechol oxidase was activated by O,1% sodium dodecyl sulfate (SDS). Catalytic power of the latent form, calculated from the kinetic parameters was 1,8 times higher than that of active one. Salicyl hydroxamic acid (SHAM) appeared as a powerful inhibitor for both active and latent forms of catechol oxidase. However, in the range of 150-250 μM SHAM the inhibitory effect for active catechol oxidase was significantly higher than that for the latent one. Non-competitive and irreversible characteristics of inhibition of latent and active catechol oxidase was calculated from kinetic data. Electrophoretic analysis followed by scanning of the gels was used. The spots' absorbance was determined from a computer image of the isoenzyme band patterns. It allowed us to estimate gels quantitatively. Presence of one additional clearly defined slow moving isoform of SDS-activated catechol oxidase, differed in the respect of 3 bands for the active and 4 bands for the total.


1965 ◽  
Vol 13 (01) ◽  
pp. 155-175 ◽  
Author(s):  
H. C Hemker ◽  
P.W Hemker ◽  
E. A Loeliger

SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.


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