Non-two-state thermal denaturation of ferricytochrome c at neutral and slightly acidic pH values

2015 ◽  
Vol 203-204 ◽  
pp. 41-50 ◽  
Author(s):  
Rastislav Varhač ◽  
Dagmar Sedláková ◽  
Marek Stupák ◽  
Erik Sedlák
Keyword(s):  
Thermal Denaturation ◽  
Acidic Ph ◽  
Ph Values ◽  
Ferricytochrome C

Is the Acidic pH of the External Auditory Canal Playing a Significant Role in the Treatment of Acute Otitis Externa?

2018 ◽  
Vol 69 (8) ◽  
pp. 2304-2305
Author(s):  
Oana Ruxandra Iana ◽  
Dragos Cristian Stefanescu ◽  
Viorel Zainea ◽  
Razvan Hainarosie
Keyword(s):  
External Auditory Canal ◽  
Otitis Externa ◽  
Proton Pumps ◽  
Acidic Ph ◽  
External Ear ◽  
Ph Values ◽  
The World ◽  
Subcutaneous Tissues ◽  
Low Levels ◽  
Value Changes

Variable pH values for skin have been reported in the literature, all within the acidic range, varying from 4.0 up to 7. 0. The origin of the acidic pH remains conjectural, and several factors have been incriminated with this role, such as eccrine and sebaceous secretions as well as proton pumps. Keeping low levels of pH prevents microbial dispersal as well as multiplication. The skin in the external auditory canal is also covered with this acidic mantle with antimicrobial value. Changes of pH in the external ear can lead to acute otitis externa. This condition is defined by the inflammation and infection of the cutaneous and subcutaneous tissues of the external auditory canal. 10% of the world�s population may suffer from acute otitis externa at least once in their lifetime. This paper aims to consolidate the relevance of an acidic pH in the healthy external ear and its relation to the pathogenesis and treatment of otitis externa through a prospective and interventional clinical study on 80 patients who presented to the outpatient department at Prof. Dr D. Hociota ENT Institute in Buch

scholarly journals In Vitro Incorporation of Helicobacter pylori into Candida albicans Caused by Acidic pH Stress

Pathogens ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 489 ◽  
Author(s):  
Kimberly Sánchez-Alonzo ◽  
Cristian Parra-Sepúlveda ◽  
Samuel Vega ◽  
Humberto Bernasconi ◽  
Víctor L. Campos ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Candida Albicans ◽  
Pcr Amplification ◽  
Growth Curves ◽  
Acidic Ph ◽  
Ph Values ◽  
16S Gene ◽  
Wide Range ◽  
H Pylori

Yeasts can adapt to a wide range of pH fluctuations (2 to 10), while Helicobacter pylori, a facultative intracellular bacterium, can adapt to a range from pH 6 to 8. This work analyzed if H. pylori J99 can protect itself from acidic pH by entering into Candida albicans ATCC 90028. Growth curves were determined for H. pylori and C. albicans at pH 3, 4, and 7. Both microorganisms were co-incubated at the same pH values, and the presence of intra-yeast bacteria was evaluated. Intra-yeast bacteria-like bodies were detected using wet mounting, and intra-yeast binding of anti-H. pylori antibodies was detected using immunofluorescence. The presence of the H. pylori rDNA 16S gene in total DNA from yeasts was demonstrated after PCR amplification. H. pylori showed larger death percentages at pH 3 and 4 than at pH 7. On the contrary, the viability of the yeast was not affected by any of the pHs evaluated. H. pylori entered into C. albicans at all the pH values assayed but to a greater extent at unfavorable pH values (pH 3 or 4, p = 0.014 and p = 0.001, respectively). In conclusion, it is possible to suggest that H. pylori can shelter itself within C. albicans under unfavorable pH conditions.

The proteoglycan region of the tumor-associated carbonic anhydrase isoform IX acts as anintrinsic buffer optimizing CO2 hydration at acidic pH values characteristic of solid tumors

2009 ◽  
Vol 19 (20) ◽  
pp. 5825-5828 ◽  
Author(s):  
Alessio Innocenti ◽  
Silvia Pastorekova ◽  
Jaromir Pastorek ◽  
Andrea Scozzafava ◽  
Giuseppina De Simone ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Solid Tumors ◽  
Acidic Ph ◽  
Ph Values

A dual-mode colorimetric/fluorescent probe based on perylene: Response to acidic pH values

2021 ◽  
Author(s):  
Liu Yang ◽  
Yan Liu ◽  
Ping Li ◽  
Yu-Long Liu ◽  
Xiao-Min Liang ◽  
...  
Keyword(s):  
Fluorescent Probe ◽  
Acidic Ph ◽  
Dual Mode ◽  
Ph Values

Orthorhombic lysozyme crystallization at acidic pH values driven by phosphate binding

2018 ◽  
Vol 74 (5) ◽  
pp. 480-489 ◽  
Author(s):  
Marina Plaza-Garrido ◽  
M. Carmen Salinas-Garcia ◽  
Ana Camara-Artigas
Keyword(s):  
Conformational Changes ◽  
Protein Function ◽  
Protein Crystallization ◽  
Amyloid Formation ◽  
Acidic Ph ◽  
Phosphate Binding ◽  
Cell Parameters ◽  
Ph Values ◽  
Phosphate Ion ◽  
Α Helix

The structure of orthorhombic lysozyme has been obtained at 298 K and pH 4.5 using sodium chloride as the precipitant and in the presence of sodium phosphate at a concentration as low as 5 mM. Crystals belonging to space groupP212121(unit-cell parametersa= 30,b= 56,c= 73 Å, α = β = γ = 90.00°) diffracted to a resolution higher than 1 Å, and the high quality of these crystals permitted the identification of a phosphate ion bound to Arg14 and His15. The binding of this ion produces long-range conformational changes affecting the loop containing Ser60–Asn74. The negatively charged phosphate ion shields the electrostatic repulsion of the positively charged arginine and histidine residues, resulting in higher stability of the phosphate-bound lysozyme. Additionally, a low-humidity orthorhombic variant was obtained at pH 4.5, and comparison with those previously obtained at pH 6.5 and 9.5 shows a 1.5 Å displacement of the fifth α-helix towards the active-site cavity, which might be relevant to protein function. Since lysozyme is broadly used as a model protein in studies related to protein crystallization and amyloid formation, these results indicate that the interaction of some anions must be considered when analysing experiments performed at acidic pH values.

scholarly journals Inactivation of tyrosine aminotransferase in neutral homogenates and rat liver slices

1972 ◽  
Vol 129 (5) ◽  
pp. 1131-1138 ◽  
Author(s):  
F. Auricchio ◽  
L. Mollica ◽  
A. Liguori
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Acid Concentration ◽  
Tyrosine Aminotransferase ◽  
Amino Acid Concentration ◽  
Acidic Ph ◽  
Ph Values ◽  
Neutral Ph ◽  
Liver Slices

Inactivation of tyrosine aminotransferase induced in vivo by triamcinolone was studied in a homogenate incubated at neutral pH values. The integrity and the presence of subcellular particles together with a compartment of acidic pH are necessary for inactivation of tyrosine aminotransferase. It is suggested that tyrosine aminotransferase is inactivated inside lysosomes. The system responsible for inactivation of tyrosine aminotransferase was partially purified and identified with lysosomal cathepsins B and B1. Inactivation of tyrosine aminotransferase in liver slices is controlled by the amino acid concentration and strongly stimulated by cysteine. 3,3′,5-Tri-iodo-l-thyronine reversibly and strongly decreases the rate of inactivation of tyrosine aminotransferase. The effect is not due to an increased rate of tyrosine aminotransferase synthesis.

scholarly journals Naphthalene diimide bis-guanidinio-carbonyl-pyrrole as a pH-switchable threading DNA intercalator

2020 ◽  
Vol 16 ◽  
pp. 2201-2211
Author(s):  
Poulami Jana ◽  
Filip Šupljika ◽  
Carsten Schmuck ◽  
Ivo Piantanida
Keyword(s):  
Thermal Denaturation ◽  
Major Groove ◽  
Groove Binding ◽  
Dna Intercalator ◽  
Dna Minor Groove ◽  
Ph Values ◽  
Naphthalene Diimide ◽  
Threading Intercalation ◽  
Neutral Conditions ◽  
Pendant Arms

A novel naphthalene diimde analogue (NDI) equipped at the imide positions with two guanidinio-carbonyl-pyrrole (GCP) pendant arms interacted significantly stronger with ds-DNA at pH 5 than at pH 7, due to reversible protonation of the GCP arms. This was consequence of a pH-switchable threading intercalation into ds-DNAs only at pH 5, while at neutral conditions (pH 7) NDI-GCP2 switched to the DNA minor groove binding. Intriguingly, NDI-GCP2 was at both pH values studied bound to the ds-RNA major groove, still showing a higher affinity and thermal denaturation effect at pH 5 due to GCP protonation. At excess over the DNA/RNA conjugate NDI-GCP2 showed also aggregation along the ds-polynucleotide and AFM and DLS demonstrated that NDI-GCP2 has pronounced ds-DNA condensation ability.

Dual sensing of glutathione and acidic pH values by using MnO2 nanosheets and 3-acetyl-7-hydroxy-2H-chromen-2-one as a fluorescent pH probe

2019 ◽  
Vol 186 (8) ◽  
Author(s):  
Lei Fu ◽  
Yanlin Du ◽  
Zhenxi Zhang ◽  
Haiyan Sun ◽  
Aixian Zheng ◽  
...  
Keyword(s):  
Acidic Ph ◽  
Mno2 Nanosheets ◽  
Ph Probe ◽  
Ph Values ◽  
Dual Sensing
Sign in / Sign up

Export Citation Format

Share Document