The pH-dependent effects of combining ethanol with fluoride on proton permeability inStreptococcus mutans

2016 ◽  
Vol 40 (4) ◽  
pp. 255 ◽  
Author(s):  
Sae-A Lee ◽  
Seung-Il Jung ◽  
Jin-Bom Kim ◽  
Jung Sook Kang
1991 ◽  
Vol 69 (5) ◽  
pp. 1116-1122 ◽  
Author(s):  
H. Miedema ◽  
H. B. A. Prins

Recently it has been hypothesized that light-induced polarity in leaves of the submerged angiosperms Potamogeton and Elodea results in part from a pH-dependent change in the permeability of the plasma membrane for protons. It is assumed that the proton permeability increases at high pH. In this paper we studied the effects on polarity of pH buffers, applied to just one side of the leaf. An experimental set up was used in which the solutions in contact with either side of the leaf surface were separated. The above hypothesis was partly confirmed, in that acidification, normally observed at the morphological lower side, was strongly suppressed by the application of a low-pH buffer at the upper side. Apparently, the low pH at the upper epidermis reduced the proton permeability, and as a result the proton pumps at the lower side were inactivated by a lack of substrate or by an effect on cytoplasmic pH. However, increasing the apoplastic pH at the lower side indicated that the proton permeability of the plasma membrane of these ceils did not change significantly. Hence both cell types seem to behave differently concerning the pH dependent proton permeability of the plasma membrane. This may explain why in the polar leaves of the angiosperms acidification always occurs at the lower and alkalinization always at the upper side. Key words: plasma membrane, proton permeability, pH polarity, Potamogeton, Elodea.


1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.


2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta

<div>Human Glycinamide ribonucleotide transformylase (GAR Tfase), a regulatory enzyme in the de novo purine biosynthesis pathway, has been established as an anti-cancer target. GAR Tfase catalyzes the formyl transfer reaction from the folate cofactor to the GAR ligand. In the present work, we study E. coli GAR Tfase, which has high sequence similarity with the human GAR Tfase with most functional residues conserved. E. coli GAR Tfase exhibits structural changes and the binding of ligands that varies with pH which leads to change the rate of the formyl transfer reaction in a pH-dependent manner. Thus, the inclusion of pH becomes essential for the study of its catalytic mechanism. Experimentally, the pH-dependence of the kinetic parameter kcat is measured to evaluate the pH-range of enzymatic activity. However, insufficient information about residues governing the pH-effects on the catalytic activity leads to ambiguous assignments of the general acid and base catalysts and consequently its catalytic mechanism. In the present work, we use pH-replica exchange molecular dynamics (pH-REMD) simulations to study the effects of pH on E. coli GAR Tfase enzyme. We identify the titratable residues governing the pH-dependent conformational changes in the system. Furthermore, we filter out the protonation states which are essential in maintaining the structural integrity, keeping the ligands bound and assisting the catalysis. We reproduce the experimental pH-activity curve by computing the population of key protonation states. Moreover, we provide a detailed description of residues governing the acidic and basic limbs of the pH-activity curve.</div>


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