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Studies of the limited degradation of mucus glycoproteins. The effect of dilute hydrogen peroxide.

ABSTRACT: 1. The action of dilute H2O2 on a series of ovarian-cyst glycoproteins and glycopolypeptides was investigated. 2. Both native glycoproteins and the glycopolypeptides were carbohydrate-rich, of relatively low molecular weight and of simple structure. 3. At pH 5.6 and 37 degrees C, exposure to H2O2 for a limited time brought about a partial degradation, the molecular weight being decreased by 2-4-fold. 4. Carbohydrate analysis showed very little change in the oligosaccharide moiety, apart from a small decrease in sialic acid in some samples. 5. Amino acid analysis showed minor changes in serine, threonine and proline contents, but almost total loss of histidine. Concomitantly, there was a small gain in aspartic acid. 6. Myosin, examined at both pH 5.7 and 6.7, exhibited generally similar behaviour, there being losses of other amino acid residues as well as histidine: the viscosity was decreased to a low value, and a range of peptides of widely varying size was produced. 7. It is suggested that attack on the histidine residue, with partial conversion into aspartic acid, is accompanied by scission of the histidyl peptide bond.

SUBMITTER: Creeth JM

PROVIDER: S-EPMC1154363 | biostudies-other | 1983 May

REPOSITORIES: biostudies-other

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Studies of the limited degradation of mucus glycoproteins. The mechanism of the peroxide reaction.

Project description:The reaction between ovarian-cyst glycoproteins and H2O2 was investigated in the presence of a number of inhibitors and catalysts. Azide and 2H2O were separately found to have little effect, implying that singlet oxygen was not involved. Superoxide dismutase was destroyed by H2O2, but mannitol had no effect: thus generalized attack by OH., whether originating from HO2.- or more directly, is not indicated. The glycoproteins contained trace quantities of Cu and Fe, amounting to about 2 atoms of metal per glycoprotein molecule. Treatment of the glycoproteins with the strong chelator DETAPAC (diethylenetriaminepenta-acetic acid) or Chelex resin eliminated the reaction with H2O2; activity could be restored by addition of Cu2+ or Fe2+ in millimolar quantities. It was concluded that metal-ion catalysis is an essential step in the attack of H2O2 on glycoproteins. Spectroscopic and other evidence showed that Cu2+ (and probably Fe2+) complexes strongly with poly-L-histidine, and implies that the Cu2+ or Fe2+ in the glycoproteins is complexed with some of the histidine residues in the glycosylated backbone. Neither polyhistidine nor polyproline reacted with H2O2 in the absence of metal ions, but small quantities of Cu2+ or Fe3+ caused degradation. This was rapid with polyhistidine, which was converted largely into aspartic acid, but slower with polyproline, where limited conversion into glutamic acid occurs. These findings confirm the original hypothesis that peroxide attack on glycoproteins occurs largely at the histidine residues, with simultaneous peptidolysis. The mechanism most probably involves the liberation of OH. by an oxidation-reduction cycle involving, e.g. Cu+/Cu2+: specificity of attack at histidine is due to the location of the metal at these residues only.

| S-EPMC1145030 | biostudies-other

Kinetic Studies on the Catalytic Degradation of Rhodamine B by Hydrogen Peroxide: Effect of Surfactant Coated and Non-Coated Iron (III) Oxide Nanoparticles.

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Structural studies on the glycoproteins from bovine cervical mucus.

Project description:The depolymerization of bovine cervical glycoprotein resulting from cleavage of disulphide bonds. Pronase digestion and both procedures sequentially was assessed by using gel filtration. Cleavage of disulphide bonds followed by Pronase digestion produced more extensive depolymerization than did either treatment alone, and gel filtration of the products resulted in two major peaks of glycosylated material on Sepharose CL-2B and Sepharose 4B. The glycopolypeptides in both peaks had similar sugar and sulphate compositions, but they migrated to different extents on gel electrophoresis. Electrophoretic studies indicated that both glycopolypeptides were derived from the same glycoprotein molecule and not from a mixture of two similar glycoproteins. Pronase digestion of glycoproteins in which the disulphide bonds had been labelled with iodo-[1-14C]acetamide revealed that most of the cysteine residues were situated in regions susceptible to Pronase. The results show the presence of two types of structural regions in bovine cervical glycoprotein, namely 'naked' peptide or non-glycosylated regions and glycopolypeptide subunit regions in which glycopolypeptides of two different sizes predominate. Comparison of the cervical glycoproteins isolated from mucus secreted during oestrus and pregnancy, by the methods outlined above, did not reveal any structural differences in the glycoproteins to explain the different physical properties of the mucus secreted under these conditions.

| S-EPMC1185863 | biostudies-other

Adaptation to hydrogen peroxide

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2009-04-23 | GSE12602 | GEO

Involvement of Polyamine Oxidase-Produced Hydrogen Peroxide during Coleorhiza-Limited Germination of Rice Seeds.

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| S-EPMC4981591 | biostudies-literature

Effect of hydrogen peroxide on Echinococcus granulosus protoescoleces proteome

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2020-05-27 | PXD015801 | Pride

Degradation of trichloroethene by siderite-catalyzed hydrogen peroxide and persulfate: Investigation of reaction mechanisms and degradation products.

Project description:A binary catalytic system, siderite-catalyzed hydrogen peroxide (H2O2) coupled with persulfate (S2O82-), was investigated for the remediation of trichloroethene (TCE) contamination. Batch experiments were conducted to investigate reaction mechanisms, oxidant decomposition rates, and degradation products. By using high performance liquid chromatography (HPLC) coupled with electron paramagnetic resonance (EPR), we identified four radicals (hydroxyl (HO·), sulfate (SO4-·), hydroperoxyl (HO2·), and superoxide (O2-·)) in the siderite-catalyzed H2O2-S2O82- system. In the absence of S2O82- (i.e., siderite-catalyzed H2O2), a majority of H2O2 was decomposed in the first hour of the experiment, resulting in the waste of HO·. The addition of S2O82- moderated the H2O2 decomposition rate, producing a more sustainable release of hydroxyl radicals that improved the treatment efficiency. Furthermore, the heat released by H2O2 decomposition accelerated the activation of S2O82-, and the resultant SO4-· was the primary oxidative agent during the first two hours of the reaction. Dichloroacetic acid was firstly detected by ion chromatography (IC). The results of this study indicate a new insight to the reaction mechanism for the catalytic binary H2O2-S2O82- oxidant system, and the delineation of radicals and the discovery of the chlorinated byproduct provide useful information for efficient treatment of chlorinated-solvent contamination in groundwater.

| S-EPMC4520253 | biostudies-literature

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2018-09-28 | E-MTAB-6627 | biostudies-arrayexpress

Do hydrogen peroxide mouthwashes have a virucidal effect? A systematic review.

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| S-EPMC7548555 | biostudies-literature

dl-Piperidinium-2-carboxyl-ate bis-(hydrogen peroxide): unusual hydrogen-bonded peroxide chains.

Project description:The title compound, C6H11NO2·2H2O2, is the richest (by molar ratio) in hydrogen peroxide among the peroxosolvates of aliphatic α-amino acids. The asymmetric unit contains a zwitterionic pipecolinic acid mol-ecule and two hydrogen peroxide mol-ecules. The two crystallographically independent hydrogen peroxide mol-ecules form a different number of hydrogen bonds: one forms two as donor and two as acceptor ([2,2] mode) and the other forms two as donor and one as acceptor ([2,1] mode). The latter hydrogen peroxide mol-ecule forms infinite hydrogen-bonded hydro-peroxo chains running along the c-axis direction, which is unusual for aliphatic α-amino acid peroxosolvates.

| S-EPMC7405570 | biostudies-literature

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