On protein interactions. XXVIII. A sedimentation study of performic acid oxidation products of chymotrypsinogen and DIP-chymotrypsin

1961 ◽  
Vol 26 (8) ◽  
pp. 2015-2021
Author(s):  
J. Šponar
Keyword(s):  
Protein Interactions ◽  
Oxidation Products ◽  
Performic Acid ◽  
Acid Oxidation

MOLECULAR WEIGHT OF BOVINE PLASMA ALBUMIN, VITELLENIN, AND THEIR OXIDATION PRODUCTS IN FORMIC ACID

1961 ◽  
Vol 39 (9) ◽  
pp. 1405-1417 ◽  
Author(s):  
W. G. Martin
Keyword(s):  
Molecular Weight ◽  
Formic Acid ◽  
Transient State ◽  
Oxidation Products ◽  
Performic Acid ◽  
Bond Rupture ◽  
Acid Oxidation ◽  
Plasma Albumin ◽  
Viscosity Measurements ◽  
Bovine Plasma

Sedimentation, diffusion, and Archibald transient state measurements were made on bovine plasma albumin and vitellenin of egg yolk in formic acid (88% w/w) solution. The molecular weight of bovine plasma albumin, averaging 77 × 103and 70 × 103with and without added salt, respectively, indicated that peptide bonds were stable to the acid for at least 1 week (storage at 5 °C and measurement periods at 20 °C). Similar values were obtained from estimates based on viscosity measurements but greater deviations occurred. Vitellenin had a mean molecular weight of 93 × 103from sedimentation and diffusion but polydispersity was revealed by the Archibald measurements (molecular weights from 55 × 103to 10 × 103). Higher values of molecular weight were obtained for vitellenin by varying the dissolution technique and exposure time in formic acid and also when viscosity measurements were used to compute molecular weight. Analyses of N-terminal amino acids showed that peptide bond rupture was not a major factor in the polydispersity of vitellenin. Although aggregates are probably present in formic acid solutions of this protein, it appears to be naturally polydisperse. Both albumin and vitellenin were considerably degraded by performic acid oxidation procedures.

scholarly journals Impact of Advanced Oxidation Products on Nanofiltration Efficiency

Water ◽  
2019 ◽  
Vol 11 (3) ◽  
pp. 541 ◽  
Author(s):  
Renata Żyłła ◽  
Rafał Milala ◽  
Irena Kamińska ◽  
Marcin Kudzin ◽  
Marta Gmurek ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Membrane Filtration ◽  
Main Product ◽  
Membrane Separation ◽  
Negative Impact ◽  
Microscopic Analysis ◽  
Contact Angles ◽  
Oxidation Products ◽  
Acid Oxidation ◽  
Dihydroxybenzoic Acid

The aim of the work was to determine the influence of salicylic acid (SA) oxidation products on the effectiveness of their further removal in the membrane filtration process. Two commercial polyamide-based polymer membranes, HL (GE Osmonics) and TS80 (TriSepTM), were used and characterized by SEM microscopic analysis, contact angles, and free surface energy. The products of salicylic acid oxidation, 2,3- and 2,5-dihydroxybenzoic acid and catechol, were determined and their impact on the removal of unreacted salicylic acid in the nanofiltration process was investigated. It was also checked to what extent and why they were retained or not by the membranes. The results of the research have shown that the main product of salicylic acid oxidation, 2,3-dihydroxybenzoic acid, has a negative impact on the retention of salicylic acid in the nanofiltration stage, while the other product, catechol, improves SA retention. The determined values of contact angles correlate well with solubility (S) of the tested compounds, which increases in the following order SSA < S2,3-DHBA < SCAT, while the contact angle of the membrane decreases. Nevertheless, it has been shown that some oxidation products can penetrate the environment due to poorer membrane separation properties of these products.

Chlorogenic Acid Oxidation by a Crude Peroxidase Preparation: Biocatalytic Characteristics and Oxidation Products

2009 ◽  
Vol 5 (1) ◽  
pp. 243-251 ◽  
Author(s):  
Ali Osman ◽  
Ayman El Agha ◽  
Dimitris P. Makris ◽  
Panagiotis Kefalas
Keyword(s):  
Chlorogenic Acid ◽  
Oxidation Products ◽  
Acid Oxidation

Ozonolysis of unsaturated fatty acids. II. Esterification of the total products from the oxidative decomposition of ozonides with 2,2-dimethoxypropane

1967 ◽  
Vol 45 (13) ◽  
pp. 1405-1410 ◽  
Author(s):  
John D. Castell ◽  
R. G. Ackman
Keyword(s):  
Fatty Acids ◽  
Liquid Chromatography ◽  
Unsaturated Fatty Acids ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Gas Liquid Chromatography ◽  
Positional Isomers ◽  
Flame Ionization ◽  
Hydrogen Flame

The total acidic products from the performic acid oxidation of the ozonide of methyl oleate formed in methanol may be esterified directly in a few hours with 2,2-dimethoxypropane. The ester concentrations are adequate for the determination of the positional isomers of monoethylenic fatty acids directly from the reaction mixture, using a hydrogen flame ionization gas–liquid chromatography detector. Dimethyl sulfoxide was not required to prevent the breakdown of 2,2-dimethoxypropane under the conditions employed.

scholarly journals Tamm–Horsfall urinary glycoprotein. The chemical composition

1970 ◽  
Vol 120 (2) ◽  
pp. 417-424 ◽  
Author(s):  
A. P. Fletcher ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Amino Acid ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Amino Acid Residues ◽  
Carbohydrate Composition ◽  
Thiol Groups ◽  
Terminal Amino Acid ◽  
Cystine Content ◽  
Terminal Amino ◽  
Urinary Glycoprotein

1. A revised amino acid and carbohydrate composition of human Tamm–Horsfall glycoprotein is presented. 2. No significant differences were obtained in the amino acid composition of Tamm–Horsfall glycoprotein isolated from patients with cystic fibrosis. 3. The glycoprotein was shown to possess a high half-cystine content of 1 per 11–12 amino acid residues, which has been confirmed by performic acid oxidation and S-alkylation with iodoacetate and iodoacetamide. No thiol groups were detected in the glycoprotein. 4. Treatment of the glycoprotein with 0.5m-sodium hydroxide at 4°C for 2 days did not release heterosaccharide material, which suggests that the predominant carbohydrate–protein linkages present are not of the O-glycosidic type. 5. No N-terminal amino acid was detected in the glycoprotein.

scholarly journals Hydrolysis of14C-labelled proteins by rumen micro-organisms and by proteolytic enzymes prepared from rumen bacteria

1983 ◽  
Vol 50 (2) ◽  
pp. 345-355 ◽  
Author(s):  
R. J. Wallace
Keyword(s):  
Proteolytic Enzymes ◽  
Rumen Fluid ◽  
Performic Acid ◽  
Cross Linking ◽  
Acid Oxidation ◽  
Rumen Bacteria ◽  
Rate Of Hydrolysis ◽  
Micro Organisms ◽  
Hydrolysis Of

1. Proteins were labelled with14C in a limited reductive methylation using [14C]formaldehyde and sodium borohydride.2. The rate of hydrolysis of purified proteins was little (< 10%) affected by methylation and the14C-labelled digestion products were not incorporated into microbial protein during a 5 h incubation with rumen fluid in vitro. It was therefore concluded that proteins labelled with14C in this way are valid substrates for study with rumen micro-organisms.3. The patterns of digestion of14C-labelled fish meal, linseed meal and groundnut-protein meal by rumen micro-organisms in vitro were similar to those found in vivo.4. The rates of hydrolysis of a number of14C-labelled proteins, including glycoprotein II and lectin from kidney beans (Phaseolus vulgaris), were determined with mixed rumen micro-organisms and with proteases extracted from rumen bacteria. Different soluble proteins were digested at quite different rates, with casein being most readily hydrolysed.5. Proteins modified by performic acid oxidation, by cross-linking using 1,6-di-iso-cyanatohexane or by diazotization were labelled with14C. Performic acid treatment generally increased the susceptibility of proteins to digestion, so that the rates of hydrolysis of performic acid-treated proteins were more comparable than those of the unmodified proteins. Cross-linking resulted in a decreased rate of hydrolysis except with the insoluble proteins, hide powder azure and elastin congo red. Diazotization had little effect on the rate of hydrolysis of lactoglobulin and albumin, but inhibited casein hydrolysis and stimulated the breakdown of γ-globulin.

Performic Acid Oxidation

2009 ◽  
pp. 841-843
Author(s):  
Alastair Aitken ◽  
Michèle Learmonth
Keyword(s):  
Performic Acid ◽  
Acid Oxidation
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