THE POLAROGRAPHY OF THE METHYL DERIVATIVES OF MALEIC HYDRAZIDE AND EXPLANATION OF THE MALEIC HYDRAZIDE WAVES

1956 ◽  
Vol 34 (12) ◽  
pp. 1760-1767 ◽  
Author(s):  
D. M. Miller

Maleic hydrazide was previously reported to have two sets of pH dependent double waves, one at low pH for which existing theories provide adequate explanation and one at higher pH for which no explanation has been offered to date. The present work is an attempt to discover the reasons for the existence of the second set of waves. An investigation of several methyl derivatives of maleic hydrazide failed to provide the desired explanation; however, a mechanism which gives a good qualitative and approximately quantitative expression for the dependence of diffusion currents and half wave potentials on pH is offered. This theory is based on the fact that succinic hydrazide, a probable product of the reduction of maleic hydrazide, has been found to have a pKa of 8.10 and thus to be present in both ionized and unionized forms over the pH range for which the double waves occur.

1986 ◽  
Vol 250 (1) ◽  
pp. R71-R76 ◽  
Author(s):  
G. P. Dobson ◽  
E. Yamamoto ◽  
P. W. Hochachka

The kinetic and regulatory properties of rabbit muscle phosphofructokinase (PFK:EC 2.7.1.11) have been reexamined in an attempt to clarify how the enzyme could achieve significant catalytic rates over the physiological pH range (down to 6.4). At 5.0 mM ATP, the apparent Km for fructose 6-phosphate (fructose 6-P) increases by at least 50-fold as the pH is decreased from 7.67 to 6.8 in 50 mM N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid-KOH buffer at 25 degrees C (7.50 to 6.63 at 37 degrees C). This effect can be nearly completely abolished in the presence of 10 microM fructose 2,6-bisphosphate (fructose 2,6-P2), with the greatest percentage change seen at low pH. In this case, the rabbit enzyme behaves as if the ATP concentration was low (1.0 mM) at any given pH. Conversely, at high ATP levels and a low pH of 6.8 at 25 degrees C, PFK behaves in the presence of fructose 2,6-P2 as if the pH has been increased to approximately 7.15 or a 0.35 pH unit shift at any given fructose 6-P concentration. At physiological concentration of fructose 6-P (0.1 mM), the positive effectors glucose 1,6-bisphosphate (glucose 1,6-P2) and either AMP, inorganic phosphate, or NH4+ were found to be, respectively, 60 and 40% as effective as fructose 2,6-P2 in reversing this pH-dependent ATP inhibition over the physiological pH range. In combination, however, glucose 1,6-P2 plus AMP were as effective as fructose 2,6-P2.(ABSTRACT TRUNCATED AT 250 WORDS)


Sensors ◽  
2020 ◽  
Vol 20 (18) ◽  
pp. 5172
Author(s):  
Ciaran K. McLoughlin ◽  
Eleni Kotroni ◽  
Mikkel Bregnhøj ◽  
Georgios Rotas ◽  
Georgios C. Vougioukalakis ◽  
...  

Fluorescein, and derivatives of fluorescein, are often used as fluorescent probes and sensors. In systems where pH is a variable, protonation/deprotonation of the molecule can influence the pertinent photophysics. Fluorination of the xanthene moiety can alter the molecule’s pKa such as to render a probe whose photophysics remains invariant over a wide pH range. Di-fluorination is often sufficient to accomplish this goal, as has been demonstrated with compounds such as Oregon Green in which the xanthene moiety is symmetrically difluorinated. In this work, we synthesized a non-symmetrical difluorinated analog of Oregon Green which we call Athens Green. We ascertained that the photophysics and photochemistry of Athens Green, including the oxygen-dependent photophysics that results in the sensitized production of singlet oxygen, O2(a1Δg), can differ appreciably from the photophysics of Oregon Green. Our data indicate that Athens Green will be a more benign fluorescent probe in systems that involve the production and removal of O2(a1Δg). These results expand the available options in the toolbox of fluorescein-based fluorophores.


1982 ◽  
Vol 85 (1) ◽  
pp. 257-263 ◽  
Author(s):  
A. Graja ◽  
M. Przybylski ◽  
B. Butka ◽  
R. Swietlik

2019 ◽  
Vol 26 (10) ◽  
pp. 743-750 ◽  
Author(s):  
Remya Radha ◽  
Sathyanarayana N. Gummadi

Background:pH is one of the decisive macromolecular properties of proteins that significantly affects enzyme structure, stability and reaction rate. Change in pH may protonate or deprotonate the side group of aminoacid residues in the protein, thereby resulting in changes in chemical and structural features. Hence studies on the kinetics of enzyme deactivation by pH are important for assessing the bio-functionality of industrial enzymes. L-asparaginase is one such important enzyme that has potent applications in cancer therapy and food industry.Objective:The objective of the study is to understand and analyze the influence of pH on deactivation and stability of Vibrio cholerae L-asparaginase.Methods:Kinetic studies were conducted to analyze the effect of pH on stability and deactivation of Vibrio cholerae L-asparaginase. Circular Dichroism (CD) and Differential Scanning Calorimetry (DSC) studies have been carried out to understand the pH-dependent conformational changes in the secondary structure of V. cholerae L-asparaginase.Results:The enzyme was found to be least stable at extreme acidic conditions (pH< 4.5) and exhibited a gradual increase in melting temperature from 40 to 81 °C within pH range of 4.0 to 7.0. Thermodynamic properties of protein were estimated and at pH 7.0 the protein exhibited ΔG37of 26.31 kcal mole-1, ΔH of 204.27 kcal mole-1 and ΔS of 574.06 cal mole-1 K-1.Conclusion:The stability and thermodynamic analysis revealed that V. cholerae L-asparaginase was highly stable over a wide range of pH, with the highest stability in the pH range of 5.0–7.0.


1974 ◽  
Vol 39 (11) ◽  
pp. 3109-3116 ◽  
Author(s):  
J. Šrogl ◽  
M. Janda ◽  
I. Stibor ◽  
V. Skála ◽  
P. Trška ◽  
...  

1972 ◽  
Vol 46 (4) ◽  
pp. 1734-1741 ◽  
Author(s):  
E. Darżynkiewicz ◽  
J.T. Kuśmierek ◽  
D. Shugar

2009 ◽  
Vol 123 (2) ◽  
pp. 146 ◽  
Author(s):  
Robert Alvo

I monitored Common Loon (Gavia immer) breeding success in relation to lake pH (range 4.0–8.5) between 1982 and 2007 on 38 single-pair lakes (5–88 ha) in the Sudbury, Ontario, area. No chicks fledged on lakes with pH < 4.4. Chicks fledged on lakes with slightly higher pH only if the lakes were relatively large. Acidic lakes became less acidic as sulphur dioxide emissions from the Sudbury smelters and sulphur deposition from other long-range sources decreased. Two lakes initially too acidic to support successful loon reproduction eventually had successful reproduction. One loon pair used two large acidic lakes (combined area 140 ha) connected by shallow rapids, and one of the adults made extremely long dives (average = 99 s) while foraging for the chicks. One chick died on that lake after apparently ingesting a very large food item; the lack of smaller items was attributed to the lake’s acidity. My results suggest that a shortage of food for chicks is the main reason why low pH reduces breeding success. I suggest that, for lakes without high levels of dissolved organic carbon (DOC), the critical pH for loon breeding success is approximately 4.3, and the suboptimal pH is approximately 4.4–6.0.


2006 ◽  
Vol 80 (17) ◽  
pp. 8830-8833 ◽  
Author(s):  
Gang Long ◽  
Xiaoyu Pan ◽  
Richard Kormelink ◽  
Just M. Vlak

ABSTRACT Entry of the budded virus form of baculoviruses into insect and mammalian cells is generally thought to occur through a low-pH-dependent endocytosis pathway, possibly through clathrin-coated pits. This insight is primarily based on (immuno)electron microscopy studies but requires biochemical support to exclude the use of other pathways. Here, we demonstrate using various inhibitors that functional entry of baculoviruses into insect and mammalian cells is primarily dependent on clathrin-mediated endocytosis. Our results further suggest that caveolae are somehow involved in baculovirus entry in mammalian cells. A caveolar endocytosis inhibitor, genistein, enhances baculovirus transduction in these cells considerably.


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