Interaction of [4-14C]Estradiol and its Metabolites with Polynucleotides in the Presence of Peroxidase

1971 ◽  
Vol 49 (8) ◽  
pp. 885-890 ◽  
Author(s):  
P. H. Jellinck ◽  
Rosemarie Fletcher
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Water Soluble ◽  
Rat Uterus ◽  
Polyadenylic Acid ◽  
Polyuridylic Acid

Incubation of [4-14C]estradiol with either horseradish peroxidase or uterine preparations resulted in the formation of water-soluble products if certain polynucleotides were also present. It was shown that both systems required hydrogen peroxide and that binding of the steroids occurred more readily with DNA or polyadenylic acid than with RNA or polyuridylic acid. The 14C radioactivity associated with the polynucleotides was present in unidentified metabolites and a small amount of unchanged estradiol. These products were bound weakly and could be removed by mild procedures in contrast to the conjugates formed with albumin or thiols by this system. The significance of the action of peroxidase in the binding of estrogens in rat uterus is discussed.

Role of 2,4-Dichlorophenol in the Oxidation of Estradiol by Uterine and Horseradish Peroxidase

1973 ◽  
Vol 51 (7) ◽  
pp. 1066-1071 ◽  
Author(s):  
C. R. Lyttle ◽  
T. McNabb ◽  
P. H. Jellinck
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Water Soluble

The role of 2,4-dichlorophenol in enhancing the conversion of [4-14C]estradiol to water-soluble products by a uterine preparation in the presence of hydrogen peroxide has been investigated. The addition of this phenol to a solution of uterine or horseradish peroxidase in 8 M urea restored the activity of the enzyme and also that of horseradish peroxidase inactivated by heating. It also protected the enzyme from inactivation during incubation. It is proposed that 2,4-dichlorophenol exerts its effect by activating peroxidase and protecting the enzyme from inactivation by the products of the reaction.

scholarly journals Inhibitory effect of retinol acetate on horseradish peroxidase

2013 ◽  
Vol 67 (3) ◽  
pp. 419-426
Author(s):  
Vladan Djuric ◽  
Nebojsa Deletic ◽  
Vesna Stankov-Jovanovic ◽  
Ranko Simonovic
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Enzymatic Reaction ◽  
Inhibitory Effect ◽  
Enzyme Concentration ◽  
Water Soluble ◽  
Primary Role ◽  
Retinol Acetate ◽  
Peroxidase Enzyme

Primary role of peroxidase enzyme is to decompose endogenous hydrogen peroxide, when oxygen radical is being replaced by a less potent radical, which is its cosubstrates oxidized form. During this study, catalytic activity of horseradish peroxidase has been observed in the presence of antioxidants from vitamin group, such as C, E and A, i.e. their water-soluble forms. It was found that vitamin E showed no effect on the enzyme activity and fate of cosubstrate radicals from the group of benzidine derivatives. Vitamin C proceeds enzymatic reaction showing its antioxidative character, and absorbs electrons from radicals, bringing cosubstrate back to its relaxed state. On the other hand, vitamin A plays a role of uncompetitive peroxidase inhibitor, which is visible through decreasing initial rate of catalytic reaction, and is reflected as virtual decrease of enzyme concentration. Furthermore, it prolongs life of endogenous hydrogen peroxide, which could potentially lead to oxidative stress of cells. This inhibitory effect can be used in analytical purpose, for determination of retinol acetate content in a sample.

Neurotoxicity and Neuroprotective Effects of Polyimides (PI) and Polyphenylenevinylene (PPV) against Hydrogen Peroxide (H2O2)

2011 ◽  
Vol 8 (2) ◽  
pp. 33
Author(s):  
Norfaezah Mazalan ◽  
Mazatulikhma Mat Zain ◽  
Nor Saliyana Jumali ◽  
Norhanim Mohalid ◽  
Zurina Shaameri ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Drug Delivery Systems ◽  
Neuronal Cells ◽  
Water Soluble ◽  
Brain Delivery ◽  
Specific Therapy ◽  
Neuroprotective Effects ◽  
Water Soluble Polymer ◽  
Site Specific ◽  
Novel Drugs

Recently, research and development in the field of drug delivery systems (DDS) facilitating site-specific therapy has reached significant progression. DDS based on polymer micelles, coated micro- and nanoparticles, and various prodrug systems including water-soluble polymer have been prepared and extensively studied as novel drugs designed for cancer chemotherapy and brain delivery. Since polymers are going to be used in human, this study has the interest of testing two types of polymer, polyimides (PI) and polyphenylenevinylene (PPV) on neuronal cells. The objective of this study was to determine the possible neurotoxicity and potential neuroprotective effects of PI and PPV towards SH-SY5Y neuronal cells challenged by hydrogen peroxide (H2O2) as an oxidant. Cells were pretreated with either PI or PPV for 1 hour followed by incubation for 24 hour with 100 µM of H2O2. MTS assay was used to assess cell viability. Results show that PI and PPV are not harmful within the concentration up to 10 µM and 100 µM, respectively. However, PI and PPV do not protect neuronal cells against toxicity induced by H2O2 or further up the cell death.

scholarly journals Monitoring the heme iron state in horseradish peroxidase to detect ultratrace amounts of hydrogen peroxide in alcohols

RSC Advances ◽  
2021 ◽  
Vol 11 (17) ◽  
pp. 9901-9910
Author(s):  
Raheleh Ravanfar ◽  
Alireza Abbaspourrad
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Oxidative Damage ◽  
Heme Iron ◽  
Aqueous Systems ◽  
Iron State ◽  
Low Concentrations

Despite the importance of hydrogen peroxide (H2O2) in initiating oxidative damage and its connection to various diseases, the detection of low concentrations of H2O2 (<10 μM) is still limited using current methods, particularly in non-aqueous systems.

scholarly journals The Reaction of Ferrous Horseradish Peroxidase with Hydrogen Peroxide

1970 ◽  
Vol 245 (9) ◽  
pp. 2409-2413
Author(s):  
Robert W. Noble ◽  
Quentin H. Gibson
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase

scholarly journals Fluorescent Derivatization of Aromatic Carboxylic Acids with Horseradish Peroxidase in the Presence of Excess Hydrogen Peroxide

2015 ◽  
Vol 31 (1) ◽  
pp. 37-44
Author(s):  
Junichi ODO ◽  
Masahiko INOGUCHI ◽  
Hiroyuki AOKI ◽  
Yuto SOGAWA ◽  
Masahiro NISHIMURA
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Carboxylic Acids ◽  
Aromatic Carboxylic Acids ◽  
Excess Hydrogen

Decoloration of Azo Dyes by Hydrogen Peroxide Catalyzed by Water-Soluble Manganese Porphyrins

1999 ◽  
Vol 69 (12) ◽  
pp. 956-960 ◽  
Author(s):  
J. Tokuda ◽  
R. Ohura ◽  
T. Iwasaki ◽  
Y. Takeuchi ◽  
A. Kashiwada ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Azo Dyes ◽  
Water Soluble ◽  
Manganese Porphyrins

scholarly journals Characterizing Wool Keratin

2009 ◽  
Vol 2009 ◽  
pp. 1-5 ◽  
Author(s):  
Jeanette M. Cardamone ◽  
Alberto Nuñez ◽  
Rafael A. Garcia ◽  
Mila Aldema-Ramos
Keyword(s):  
Hydrogen Peroxide ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Alkaline Solutions ◽  
Biodegradable Material ◽  
Alkaline Hydrogen Peroxide ◽  
Cortical Cells ◽  
Sds Page ◽  
Fibrous Matrices ◽  
Wool Keratin

Keratin from wool is a reactive, biocompatible, and biodegradable material. As the biological structural component of skin (soft keratins) and of nails, claws, hair, horn, feathers, and scales (hard keratins) pure keratin comprises up to 90% by weight of wool. Wool was treated in alkaline solutions to extract from 68% to 82% keratin within 2 to 5 hours of exposure at . The keratin products were water-soluble and were confirmed to contain intermediate filament and microfibrillar component-proteins of fractured, residual cuticle, and cortical cells. Oxidation of wool by peroxycarboximidic acid in alkaline hydrogen peroxide produced keratin products with distinct microcrystalline structures: descaled fibers, fibrous matrices, and lyophilized powders. Morphology and confirmation of peptide functionality were documented by SEM, Amino Acid Analysis, SDS-PAGE gel electrophoresis, MALDI-TOF/TOF, and FTIR analyses. The reactivity of keratin from wool models the reactivity of keratin from low-value sources such as cattle hair.

scholarly journals Polyribonucleotide synthesis by subfractions of microsomes from rat liver

1968 ◽  
Vol 109 (2) ◽  
pp. 229-238 ◽  
Author(s):  
N. M. Wilkie ◽  
R. M. S. Smellie
Keyword(s):  
Acetic Acid ◽  
Rat Liver ◽  
Transfer Rna ◽  
Light Fraction ◽  
Free Ribosome ◽  
Polyadenylic Acid ◽  
Insoluble Material ◽  
Polyuridylic Acid ◽  
Microsome Fraction

1. The microsome fraction of rat liver has been fractionated and the ability of the fractions to incorporate ribonucleotides into polyribonucleotides has been studied. Activity was found in the rough-surfaced vesicle (light) fraction and in the free-ribosome fraction and this latter activity has been examined. 2. The free-ribosome fraction contains ribosome monomers, dimers and trimers together with some higher oligomers and ferritin. In addition to catalysing the incorporation of ribonucleotides into acid-insoluble material it contains diesterase activity. It catalyses the incorporation of UMP from UTP, but not UDP, AMP from ATP and CMP from CTP into polyribonucleotide material, and for UTP the product appears to be a homopolymer not more than eight units long attached to the ends of primer polyribonucleotide strands. 3. The activity could not be removed from the free-ribosome fraction by washing or by isolation in the presence of ethylenediaminetetra-acetic acid. 4. Partially hydrolysed polyuridylic acid but not polyadenylic acid could serve as a primer for the incorporation of UMP, but some activity was always associated with an endogenous primer. 5. Analysis of RNA extracted from the free-ribosome fraction after incubation with [3H]UTP showed the presence of 28s, 18s, 5s and transfer RNA types, but no radioactivity was associated with any of these RNA fractions.

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