MODIFICATION OF OZONE DAMAGE TO PHASEOLUS VULGARIS BY ANTIOXIDANTS, THIOLS AND SULFHYDRYL REAGENTS

1968 ◽  
Vol 48 (6) ◽  
pp. 569-574 ◽  
Author(s):  
H. C. Dass ◽  
G. M. Weaver
Keyword(s):  
Ascorbic Acid ◽  
Phaseolus Vulgaris ◽  
Lactic Dehydrogenase ◽  
Sulfhydryl Reagents ◽  
Thiol Compounds ◽  
Ozone Injury ◽  
Ozone Sensitivity ◽  
Cysteine Hydrochloride ◽  
White Bean

Representative cultivars of white bean (Phaseolus vulgaris) were treated with selected antioxidants, thiol compounds and sulfhydryl reagents and then exposed to ozone under laboratory conditions. Severity of the bronzing disorder was influenced by such treatments, as was the activity of peroxidase and lactic dehydrogenase enzymes.Dust applications of ascorbic acid and nickel-N-dibutyl dithiocarbamate markedly reduced ozone injury, the latter compound being the most effective. Decreased ozone sensitivity was also noted following treatment of a susceptible and a tolerant cultivar with cysteine hydrochloride and glutathione.The severity of bronzing was increased over that of the control plants by the application of sulfhydryl reagents, namely parachloromercuribenzoate and N-ethyl maleimide. Necrotic stipple of the upper surface of the lamina, a symptom associated with the bronzing disorder, was induced following treatment with the sulfhydryl reagents without exposure to ozone.Ozone fumigation increased peroxidase activity and decreased lactic dehydrogenase activity. Similar effects were observed following treatment with parachloromercuribenzoate. Neither enzyme showed response to the application of cysteine hydrochloride.The role of protein sulfhydryls is discussed in relation to ozone damage and the bronzing disorder.

scholarly journals ON THE ROLE OF VIRUS SULFHYDRYL GROUPS IN THE ATTACHMENT OF ENTEROVIRUSES TO ERYTHROCYTES

1960 ◽  
Vol 112 (3) ◽  
pp. 455-478 ◽  
Author(s):  
Lennart Philipson ◽  
Purnell W. Choppin
Keyword(s):  
Virus Particle ◽  
Human Erythrocytes ◽  
Hemagglutinating Activity ◽  
Sulfhydryl Groups ◽  
Present Communication ◽  
Sulfhydryl Reagents ◽  
Thiol Compounds ◽  
Virus Particles ◽  
Receptor Sites

Many animal viruses possess the ability to agglutinate erythrocytes. In most but not all cases hemagglutination is due to the virus particle itself, and appears to result from the mechanical bridging of two or more erythrocytes by virus particles which attach to receptor sites on each erythrocyte (1, 2). Thus, attachment of virus particles to erythrocytes is a prerequisite for hemagglutination, and prevention of absorption of virus prevents hemagglutination. Among the enteroviruses, many ECHO viruses and some strains of Coxsackie B3 virus agglutinate human erythrocytes (3-7), and the evidence indicates that hemagglutination is due to the virus particle itself (3, 5, 6). The precise mechanism of attachment of enteroviruses to cells is unknown. Chymotrypsin treatment of erythrocytes prevents the absorption of some ECHO viruses (8). This suggests that the receptor sites on the erythrocyte may be at least in part protein in nature. The present communication is concerned with the mechanism of attachment of enteroviruses to cells. It is shown that sulfhydryl reagents block the hemagglutinating activity of enteroviruses. Treated virus fails to absorb to erythrocytes. Thiol compounds restore the hemagglutinating activity of enteroviruses treated with mercaptide-forming sulfhydryl reagents. The effect of sulfhydryl reagents on the infectivity of some enteroviruses is also described.

scholarly journals Ascorbic Acid and Ozone: Novel Perspectives to Explain an Elusive Relationship

Plants ◽  
2019 ◽  
Vol 8 (5) ◽  
pp. 122 ◽  
Author(s):  
Erika Bellini ◽  
Mario C. De Tullio
Keyword(s):  
Ascorbic Acid ◽  
Biosynthetic Pathway ◽  
Regulation Of Gene Expression ◽  
Physiological Role ◽  
Total Content ◽  
Huge Amount ◽  
Ozone Sensitivity ◽  
Ozone Tolerance ◽  
The Relationship

A huge amount of studies highlighted the importance of high ascorbic acid (AA) content in ozone tolerance, yet the relationship between them appears more complex than a simple direct correlation. Sometimes the connection is clear, for example, two Arabidopsis mutants defective in the main AA biosynthetic pathway (vtc mutants) were identified by means of their ozone sensitivity. However, some low-AA containing mutants are relatively tolerant, suggesting that AA location/availability could be more relevant than total content. A clear distinction should also be made between ozone tolerance obtained when AA content is increased by experimental supplementation (exogenous AA), and the physiological role of plant-synthesized AA (endogenous AA), whose amount is apparently subjected to tight regulation. Recent findings about the role of AA in signal transduction and epigenetic regulation of gene expression open new routes to further research.

ĐIỀU TRA, TINH SẠCH VÀ TÌM HIỂU TÍNH CHẤT ĐẶC TRƯNG CỦA LECTIN MỘT SỐ GIỐNG ĐẬU CÔ VE (PHASEOLUS VULGARIS L.)

2013 ◽  
Vol 75 (6) ◽  
Author(s):  
Cao Đăng Nguyên ◽  
Nguyễn Thị Cẩm Hạnh
Keyword(s):  
Phaseolus Vulgaris ◽  
Phaseolus Vulgaris L ◽  
White Bean

Đã điều tra lectin của 6 giống đậu cô ve thấy rằng cả 6 giống đều có hoạt tính lectin trong đó giống đậu cove hạt trắng dạng bụi (white bean core bush type white seeds) có hoạt tính lectin mạnh nhất, đặc biệt đối với hồng cầu trâu, bò, lợn. Lectin của 6 giống này đều không có biểu hiện đặc hiệu nhóm máu. Lectin đậu cove hạt trắng dạng bụi hoạt động tốt nhất ở nhiệt độ 300C – 400C, pH 6,8 – 7,6. Các đường α-D-glucose, α-D-galactose, D-mannose, D-fructose, D-saccharide,  D-lactose, D-arabinose và D-manitose ở nồng độ 0,05 – 0,1 M có tác dụng kìm hãm hoạt tính của lectin đậu cove hạt trắng dạng bụi. Lectin này cũng bị kìm hãm bởi protein của một số huyết thanh người và động vật (trâu, bò, lợn). Đã tinh sạch lectin đậu cove hạt trắng dạng bụi có độ tinh sạch gấp khoảng 52 lần so với dịch thô ban đầu. Trên gel polyacrylamide thấy xuất hiện 5 band có khối lượng phân tử trong khoảng 30 – 97 kDa.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

Ambivalent role of ascorbic acid in the metal-catalyzed oxidation of oligopeptides

2021 ◽  
pp. 111510
Author(s):  
Nikolett Bodnár ◽  
Katalin Várnagy ◽  
Lajos Nagy ◽  
Gizella Csire ◽  
Csilla Kállay
Keyword(s):  
Ascorbic Acid ◽  
Metal Catalyzed Oxidation ◽  
Metal Catalyzed ◽  
Catalyzed Oxidation

scholarly journals The role of ascorbic acid combined exposure on Imidacloprid-induced oxidative stress and genotoxicity in Nile tilapia

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Islam M. El-Garawani ◽  
Elsayed A. Khallaf ◽  
Alaa A. Alne-na-ei ◽  
Rehab G. Elgendy ◽  
Gaber A. M. Mersal ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ascorbic Acid ◽  
Nile Tilapia ◽  
Protective Agent ◽  
Strand Breaks ◽  
Gill Cells ◽  
Significant Amelioration ◽  
Neonicotinoid Insecticide ◽  
Dna Strand

AbstractImidacloprid (Imid), a systemic neonicotinoid insecticide, is broadly used worldwide. It is reported to contaminate aquatic systems. This study was proposed to evaluate oxidative stress and genotoxicity of Imid on Nile tilapia (Oreochromis niloticus) and the protective effect of ascorbic acid (Asc). O. niloticus juveniles (30.4 ± 9.3 g, 11.9 ± 1.3 cm) were divided into six groups (n = 10/replicate). For 21 days, two groups were exposed to sub-lethal concentrations of Imid (8.75 ppm, 1/20 of 72 h-LC50 and 17.5 ppm, 1/10 of 72 h-LC50); other two groups were exposed to Asc (50 ppm) in combination with Imid (8.75 and 17.5 ppm); one group was exposed to Asc (50 ppm) in addition to a group of unexposed fish which served as controls. Oxidative stress was assessed in the liver where the level of enzymatic activities including superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) in addition to mRNA transcripts and, Lipid peroxidation (LPO) were evaluated. Moreover, mitotic index (MI) and comet assay were performed, in addition, the erythrocytic micronucleus (MN), and nuclear abnormalities (NA) were observed to assess genotoxicity in fish. Imid exposure induced significant (p ˂ 0.05) changes in the antioxidant profile of the juveniles' liver by increasing the activities and gene expression of SOD, CAT and GPX as well as elevating the levels of LPO. DNA strand breaks in gill cells, erythrocytes and hepatocytes along with erythrocytic MN and NA were also significantly elevated in Imid-exposed groups. MI showed a significant (p ˂ 0.05) decrease associated with Imid exposure. Asc administration induced a significant amelioration towards the Imid toxicity (8.75 and 17.5 ppm). A significant protective potency against the genotoxic effects of Imid was evidenced in Asc co-treated groups. Collectively, results highlight the importance of Asc as a protective agent against Imid-induced oxidative stress and genotoxicity in O. niloticus juveniles.

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