Effect of phosphate buffer on the kinetics of glycation of proteins

2005 ◽  
Vol 18 (2) ◽  
pp. 183-186 ◽  
Author(s):  
Herminia Gil ◽  
Daniel Salcedo ◽  
Rom�n Romero
Keyword(s):  
Phosphate Buffer ◽  
Kinetics Of

Viral inactivation by potassium ferrate

1995 ◽  
Vol 31 (5-6) ◽  
pp. 165-168 ◽  
Author(s):  
Futaba Kazama
Keyword(s):  
Phosphate Buffer ◽  
Potassium Ferrate ◽  
Sodium Thiosulphate ◽  
Viral Inactivation ◽  
Complete Decomposition ◽  
Kinetics Of ◽  
Oxidative Intermediate

The kinetics of inactivation by potassium ferrate were studied using a bacteriophage, F-specific RNA-coliphage Qβ as a viral model. The inactivation appeared to be expressed by Hom's model in phosphate buffer at pH 6, 7, and 8. The rate of inactivation depended on pH; the lower pH, the faster inactivation observed. To consider the mechanism by which ferrate caused inactivation, the efficiency of inactivation was checked after ferrate decomposition in buffer. Effective inactivation following Hom's model was also observed after the complete decomposition of ferrate ion; however, the efficiency of that inactivation disappeared by the addition of sodium thiosulphate, suggesting that rather long-lived oxidative intermediate was generated by the decomposition of ferrate ion. The intermediate might take part in the inactivation.

scholarly journals DETECTION OF HYDROPEROXIDES IN SOLUTIONS OF PHOTOOXIDIZED PSORALEN

2019 ◽  
Vol 14 (1) ◽  
pp. 32-38
Author(s):  
V. V. Skarga ◽  
E. V. Nevezhin ◽  
A. А. Matrosov ◽  
V. V. Negrebetsky ◽  
M. V. Malakhov
Keyword(s):  
Quantitative Analysis ◽  
Phosphate Buffer ◽  
Biological Effects ◽  
Xylenol Orange ◽  
Phosphate Buffer Solution ◽  
Buffer Solution ◽  
Uva Irradiation ◽  
Fox Assay ◽  
Kinetics Of ◽  
Ferrous Oxidation

Photooxidized psoralen solutions possess a variety of biological effects, which implementation mechanism may presumably involve hydroperoxides. Here, the hydroperoxide content in photooxidized psoralen solutions was assessed using photometric FOX assay (from Ferrous Oxidation + Xylenol Orange). FOX reagent with 10× content of Xylenol Orange, modified for quantitative analysis of up to 50 μM of hydroperoxides in aqueous phase was used in experiments. During photooxidation of 0.1 mM psoralen in phosphate buffer solution, hydroperoxide production increases with dose of UVA irradiation (~2.5 μM eq. of H2O2 for dose of 252 kJ/m2 and ~11 μM eq. of H2O2 for dose of 1512 kJ/m2) and reaches ~16.5 μM eq. of H2O2 at the highest dose investigated (3024 kJ/m2). A comparison of kinetics of psoralen photolysis and hydroperoxide generation allows us to suggest that generation of hydroperoxide results from the secondary photochemical processes involving psoralen photoproducts, presumably from photoinduced autooxidation of aldehydic photoproducts of psoralen.

scholarly journals Kinetics of the heat insolubilisation of soybean 11S protein in a phosphate buffer system.

1988 ◽  
Vol 52 (8) ◽  
pp. 2095-2096 ◽  
Author(s):  
Ken WATANABE
Keyword(s):  
Phosphate Buffer ◽  
Buffer System ◽  
Kinetics Of

scholarly journals Hypochlorite inactivation kinetics of Listeria monocytogenes in phosphate buffer

2004 ◽  
Vol 159 (2) ◽  
pp. 167-171 ◽  
Author(s):  
Osman Erkmen
Keyword(s):  
Listeria Monocytogenes ◽  
Phosphate Buffer ◽  
Inactivation Kinetics ◽  
Kinetics Of

Inhibition of Hb S Polymerization In Vitro by a Novel EF Helix ß73 His Containing Peptide.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3569-3569
Author(s):  
Mohammed G.K. Akbar ◽  
Min Ding ◽  
Saul Surrey ◽  
Kazuhiko Adachi
Keyword(s):  
Hydrogen Bond ◽  
Amino Acid ◽  
Phosphate Buffer ◽  
Elongation Rate ◽  
Fiber Elongation ◽  
Kinetics Of Polymerization ◽  
Molar Excess ◽  
Hb S ◽  
Kinetics Of ◽  
Hb C

Abstract Sickle hemoglobin polymerization involves not only ß6 Val in a largely hydrophobic acceptor pocket but other contact sites. We recently found that the ß73 His Hb S variant (ß6 Val and ß73 His) promoted polymerization compared to deoxy Hb S, while ß73 Leu Hb S (ß6 Val and ß73 Leu) inhibited polymerization like deoxy Hb C-Harlem (ß6 Val and ß73 Asn). In fact, ß73 Asp in Hb S makes a hydrogen bond with ß4 Thr in deoxy Hb S polymers, and this is a unique position to promote or inhibit polymerization by amino acid change [Adachi et al., Biochemistry (2003), 42, 4476]. Kinetics of polymerization, solubility and minimum concentration required for polymerization of the ß73 Hb S variants were affected by ß73 amino acid (inhibition of polymerization: His < <Asp <<Asn < Leu). Inhibition of Hb S ß73 Leu polymerization compared to Hb S may be caused by weakening of the hydrogen bond interaction between the hydroxyl group of ß4 Thr and the ß73 amino acid like Hb C-Harlem. Furthermore, kinetics of polymerization of 1:1 Hb S/Hb A ß73 His mixtures were enhanced compared to AS mixtures, while Hb S/Hb A ß73 Leu mixtures showed inhibitory effects similar to FS mixtures. These results suggest that the Hb A ß73His variant promotes Hb S polymerization almost as efficiently as Hb S ß73 His, and that the ß73 His in Hb A and Hb S variants strengthens the hydrogen bond with ß4 Thr, which helps facilitate formation of domains and 14-stranded fibers. Based on these results, we chemically synthesized a 15-mer EF helix peptide containing ß73 His (Lys-Lys-Val-Leu-Gly-Ala-Phe-Ser-His-Gly-Leu-Ala-His-Leu-Asp) and evaluated effects of this peptide on Hb S polymerization. DIC analysis in 1.0 M phosphate buffer showed peptide-induced inhibition of fiber elongation rate for deoxy-Hb S which increased linearly with increasing amounts of peptide (e.g., a 5-fold molar excess of peptide resulted in a 6-fold decrease in fiber elongation rate). Solubility of deoxy Hb S increased linearly with increasing peptide (e.g., a 5-fold molar excess of peptide increased solubility by 1.2-fold). The delay time prior to polymerization of deoxy Hb S in a high phosphate buffer also was increased significantly in the presence of this peptide. In contrast, the same 15-mer peptide containing ß73 Leu instead of His showed no effect on solubility or kinetics of polymerization, suggesting that the ß73 His peptide specifically affects the A-helix of Hb S containing ß4 Thr just like the ß73 His Hb S variant. This and possibly other peptides interrupting the ß73-ß4 interaction which result in inhibition of deoxy Hb S polymerization may be good candidates for inhibitors of Hb S polymerization.

Kinetics of the chromium(VI)-arsenic(III)reaction. II. Dihydrogen phosphate-hydrogen phosphate buffer solutions

1970 ◽  
Vol 9 (4) ◽  
pp. 847-850 ◽  
Author(s):  
John G. Mason ◽  
Albert D. Kowalak ◽  
R. Michael Tuggle
Keyword(s):  
Phosphate Buffer ◽  
Dihydrogen Phosphate ◽  
Hydrogen Phosphate ◽  
Buffer Solutions ◽  
Chromium Vi ◽  
Kinetics Of

Degradation kinetics of poly(lactic-co-glycolic) acid block copolymer cast films in phosphate buffer solution as revealed by infrared and Raman spectroscopies

2011 ◽  
Vol 96 (10) ◽  
pp. 1882-1889 ◽  
Author(s):  
Elisabeth Vey ◽  
Caroline Rodger ◽  
Jonathan Booth ◽  
Mike Claybourn ◽  
Aline F. Miller ◽  
...  
Keyword(s):  
Block Copolymer ◽  
Phosphate Buffer ◽  
Glycolic Acid ◽  
Degradation Kinetics ◽  
Phosphate Buffer Solution ◽  
Buffer Solution ◽  
Cast Films ◽  
Kinetics Of

Amperometric Study of the Kinetics of Exocytosis in Mouse Adrenal Slice Chromaffin Cells: Physiological and Methodological Insights

2006 ◽  
Vol 96 (3) ◽  
pp. 1196-1202 ◽  
Author(s):  
Gloria Arroyo ◽  
Jorge Fuentealba ◽  
Natalia Sevane-Fernández ◽  
Marcos Aldea ◽  
Antonio G. García ◽  
...  
Keyword(s):  
Electrical Stimulation ◽  
Carbon Fiber ◽  
Phosphate Buffer ◽  
Neurotransmitter Release ◽  
Chromaffin Cells ◽  
Nicotinic Receptors ◽  
Adrenal Glands ◽  
Splanchnic Nerve ◽  
Amperometric Response ◽  
Kinetics Of

This study was designed to examine the kinetics of neurotransmitter release using the carbon fiber amperometric technique on cells in slices of mouse adrenal glands superfused with bicarbonate phosphate buffer–based solutions. The exocytotic amperometric response evoked by electrical stimulation was significantly faster than that produced after exogenous application of ACh or K+. Splanchnic nerve–evoked neurotransmitter release was blocked by hexamethonium, indicating the involvement of ACh nicotinic receptors. We discuss the implications of our data for understanding the mechanisms underlying the vesicle fusion process.

Sign in / Sign up

Export Citation Format

Share Document