Phenylmercuric Acetate Research Articles

Mercury binding to proteins disclosed by ESI MS experiments: The case of three organomercurials

Solution interactions of three organomercury compounds, i.e., methylmercury chloride, thimerosal and phenylmercury acetate, with a group of biochemically relevant proteins, namely cytochrome c (Cyt c), ribonuclease A (RNase A), carbonic anhydrase I (hCA I), superoxide dismutase (SOD), and serum albumin (HSA), were investigated using an established ESI MS approach. Temporal analysis of sample aliquots provided insight into the binding kinetics, while comparative analysis of the obtained mass spectra disclosed adduct formation of each mercurial with the tested proteins and the relative abundance of the species. The three organomercurials bind, exclusively and tightly, to free cysteine residues as no binding was observed in the case of proteins lacking such groups. hCA I, SOD and HSA formed distinct mercury adducts, preserving the Hg bound alkyl/aryl ligands; yet, the three organomercurials displayed significant differences in reactivity in relation to their chemical structure. The investigation was then extended to analyze the reactions with the C-terminal dodecapeptide of the enzyme human thioredoxin reductase, which contains a characteristic selenol-thiol moiety: tight Hg binding was observed. Notably, this peptide was able to remove effectively and completely the alkyl/aryl ligands of the three tested organomercurials; this behavior may be relevant to the detoxification mechanism of organomercurials in mammals. Finally, a competition experiment was carried out to establish whether protein bound mercury centers may be displaced by other competing metals. Interestingly, and quite unexpectedly, we observed that a protein bound mercury fragment may be partially displaced from its coordination site in hCA I by the medicinal gold compound auranofin.

Synthesis, spectroscopic and hydrogen storage studies of mono or bimercury(II) mixed ligand complexes of amines with 2-cyanoamino thiophenolate ligand

Organic heterocyclic compounds play a significant role in coordination chemistry due to their ability to act as donor atoms for coordinating with various metal or metal ions. In this study, particular attention was given to the conversion of the 2-aminobenzothiazole ligand into 2-cyanoaminothiophenolate (LH) through a ring-breaking reaction. This transformation was achieved by reacting 2-aminobenzothiazole with phenyl mercury(II) acetate in the presence of sodium hydroxide, resulting in the formation of the complex [pHHg(LH)]n. During this process, mono-deprotonation of 2-aminobenzothiazole occurred, accompanied by facial carbon-sulfur bond breaking. This complex was used as a synthon to prepare four new mononuclear and binuclear complexes, which were [pHHg(LH)(apmy)2] (apmy= 2-aminopyrimidine) and [PhHg(LH)(bipy)] and [pHHg(LH)(μ-Cl)2Hg(bipy)] and [pHHg(LH)(μ-Cl)2Hg(phen)]. The prepared complexes were characterized using melting point, elemental analysis, FTIR, 1HNMR and 13CNMR. The results showed that the 2-cyanoamino thiophenolate ligand exhibited a monodentate behavior across the thiol sulfur atom, while the nitrile group remained free. The complex [pHHg(LH)(μ-Cl)2Hg(phen)] was used to study its ability to store hydrogen at different temperatures in order to study the thermodynamic parameters (enthalpy and entropy). The study proved that the highest stored value was 1.92 wt.% H2. It was noted that this ratio can be stored at lower pressures as the temperature decreases, proving that the storage is of a physical type with the value of R2= 0.92602 for the Van't Hof plot. The enthalpy value was 0.1131118 (kJ/(mol H2) while the entropy value was 0.60649754 (J/mol H2. K).

Allergic Complications of Hyaluronidase Injection: Risk Factors, Treatment Strategies, and Recommendations for Management.

Hyaluronidase is used as a reversal agent for hyaluronic acid fillers and to increase the diffusion of other medications after infiltration. Cases of hyaluronidase allergy have been described in the literature since 1984. However, it is still frequently misdiagnosed. This review aims to summarize the current literature to describe the clinical picture of hyaluronidase allergy and identify any risk factors associated with its development, as well as provide recommendations for management in plastic surgery. A digital search of PubMed, Scopus, and Embase databases was performed by two reviewers following the PRISMA guidelines. This search identified 247 articles. Two hundred forty-seven articles were identified, and 37 of them met the eligibility criteria. One hundred six patients with a mean age of 54.2 years were included in these studies. History of allergy to other substances (timothy grass, egg white, horse serum, penicillin, insect bites, wasp venom, thimerosal, potassium, histamine, phenylmercuric acetate, and nickel) and allergic diseases (asthma, dermatitis, atopy, rhinitis) was reported. A large portion of the patients with a history of repeated exposure (2-4) experienced the symptoms with their second injection. Nonetheless, there was no significant association between time to allergy development and the number of exposures (P = 0.3). Treatment with steroids +/- antihistamines resulted in the rapid and predominantly complete reversal of the symptoms. Prior injections or sensitization by insect/wasp venom might be the primary factor associated with hyaluronidase allergy development. The time between the repeated injections is not a likely contributor to the presentation. This journal requires that authors assign a level of evidence to each article. For a full description of these Evidence-Based Medicine ratings, please refer to the Table of Contents or the online Instructions to Authors www.springer.com/00266 .

Synthesis and characterization of unsymmetrical Selenoethers: Facile cleavage of the Se-C bond

Installation of in situ generated arylselenide (ArSe-) on 2‑methyl napthalene afforded the following selenoethers: 2-C10H7CH2Se(C6H5), 2-C10H7CH2Se(p-CH3C6H5), 2-C10H7CH2Se(1-C10H7) and 2-C10H7CH2Se(2,4,6-Me3C6H2), as yellow crystalline solids. These molecules can be prepared by the treatment of in situ generated arylselenide with 2-C10H7CH2Br in ethanol solvent at 0 °C in excellent yield. These molecules are characterized by 1H, 13C, 77Se NMR and elemental analysis. Among these, 2-C10H7CH2Se(C6H5) and 2-C10H7CH2Se(2,4,6-Me3C6H2) are also characterized by single-crystal X-ray studies. Phenyl mercury acetate was isolated in good yield through the treatment of 2-C10H7CH2Se(C6H5) with mercuric acetate. In this reaction cleavage of the C(aryl)–Se bond takes place. Similarly, 2-C10H7CH2Se(C6H5) and 2-C10H7CH2Se(p-CH3C6H5) also exhibited cleavage of the C(aryl)–Se bond with HgCl2 and afforded [2-C10H7CH2Se(C6H5)(C6H5HgCl)] and [2-C10H7CH2Se(p-MeC6H4)(p-MeC6H4HgCl)] complexes in good yield respectively. A organopalladium(II) complex, [3-C10H6PdCl(2-CH2SeC6H5)]2, was also developed through the reaction of 2-C10H7CH2Se(C6H5) with Na2PdCl4.

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Genotoxicity of Mercury and Its Derivatives Demonstrated In Vitro and In Vivo in Human Populations Studies. Systematic Review.

Beside partial coverage in three reviews so far (1994, 2009, 2019), there is no review on genotoxic studies dealing with mercury (Hg) and human exposure using the most usual genotoxic assays: sister chromatid exchanges (SCE), chromosomal aberrations (CA), cytochalasin B blocked micronucleus assay (CBMN), and single-cell gel electrophoresis (SCGE or alkaline comet assay). Fifty years from the first Hg genotoxicity study and with the Minamata Convention in force, the genotoxic potential of Hg and its derivatives is still controversial. Considering these antecedents, we present this first systematic literature overview of genotoxic studies dealing with Hg and human exposure that used the standard genotoxic assays. To date, there is not sufficient evidence for Hg human carcinogen classification, so the new data collections can be of great help. A review was made of the studies available (those published before the end of October 2021 on PubMed or Web of Science in English or Spanish language) in the scientific literature dealing with genotoxic assays and human sample exposure ex vivo, in vivo, and in vitro. Results from a total of 66 articles selected are presented. Organic (o)Hg compounds were more toxic than inorganic and/or elemental ones, without ruling out that all represent a risk. The most studied inorganic (i)Hg compounds in populations exposed accidentally, occupationally, or iatrogenically, and/or in human cells, were Hg chloride and Hg nitrate and of the organic compounds, were methylmercury, thimerosal, methylmercury chloride, phenylmercuric acetate, and methylmercury hydroxide.

Successful expression of the synthetic merBps gene in tobacco

Organomercury is the most toxic biomagnifiable state of mercury, and to date, no natural organomercurial detoxification mechanism is encountered in plants. Bacterial merB gene encoding organomercury lyase show low expression in transgenic plants. For ideal expression, a synthetic merBps gene possessing143 out of 213 codons discrete from native merB gene from Escherichia. coli was fabricated based on codon usage in tobacco. Through Agrobacterium-mediated transformation, the merBps gene got successfully integrated into tobacco. Of several putative merBps transformants selected with 200 μg ml-1 kanamycin, only ∼45% were PCR positive for both nptII and merBps genes. Healthy and vigorously growing shoots of few PCR-positive putative transgenic lines were multiplied and rooted. After transplantation and acclimatization, the resultant plants flowered and fruited in pots. Southern analysis revealed the presence of a single copy of the merBps gene in four lines. RT-PCR and Western investigations established successful transcription and translation of the merBps gene in these transgenic lines, respectively. Fabrication of fully functional organomercury lyase in merBps transgenic lines was established based on the potential of their (i) seeds to germinate; (ii) shoots to grow and multiply; and (iii) leaf disc to remain green, even in the presence of 4 nmole ml-1 phenylmercuryacetate (PMA) while the wild type was susceptible to even 1 nmole ml-1 PMA. These findings confirmed that the synthetic merBps gene could be effectively expressed in plants and exploited for remediation of organomercurial contaminated sites.

Mercury(II) mixed ligand complexes of phosphines or amines with 2-cyanoamino thiophenolate ligands formed via monodeprotonation and carbon–sulfur bond cleavage of 2-aminobenzothiazole. X-ray crystal structures of [Hg(SC6H4NCN)(PPh3)]2 and [Hg(SC6H4NCN)(Ph2PCH2PPh2)

The addition of sodium hydroxide to a mixture of phenyl mercury acetate and 2-aminobenzothiazole in warm ethanol led to the high yield (84%) formation of [Ph-Hg(LH)]n (1), LH = the 2-cyanoaminothiaphenolate anion (SC6H4NHCN)−, resulting from monodeprotonation of 2-aminobenzothiazole and facile carbon–sulfur bond breakage. Reaction of 1 with Ph3P or Ph3PS afforded [Hg(LH)2(Ph3P)2] (2) or [PhHg(μ-LH)(Ph3PS)]2 (3), respectively. Recrystallization of 2 from warm DMSO afforded [Hg(μ-L)(PPh3)]2 (4), L = the 2-cyanoaminothiophenolate di-anion (SC6H4NCN)2−, which was characterized by an X-ray diffraction study. Treatment of 1 with the diphosphines Ph2P(CH2)nPPh2, 2,6-diaminopyridine (dapy), ethylenediamine (en) or 1,10-phenanthroline (phen) afforded [PhHg(LH){ Ph2P(CH2)nPPh2}], {n = 1 dppm (5), n = 2 dppe (6), n = 3 dppp (7), n = 4 dppb (8), (CH2)n = (Cp)2Fe dppf (9)}, [PhHg(LH)(dapy)2] (11), [PhHg(LH)(en)] (12) or [PhHg(LH)(phen)] (13). Recrystallization of 5 from CH2Cl2 afforded the binuclear complex [Hg(μ-L)(η1-dppm)]2.CH2Cl2 (10), which has been characterized by an X-ray diffraction study.

Biochemical screening for SARS-CoV-2 main protease inhibitors.

The Severe Acute Respiratory Syndrome Corona Virus 2 (SARS-CoV-2) pandemic represents a global challenge. SARS-CoV-2's ability to replicate in host cells relies on the action of its non-structural proteins, like its main protease (Mpro). This cysteine protease acts by processing the viruses' precursor polyproteins. As proteases, together with polymerases, are main targets of antiviral drug design, we here have performed biochemical high throughput screening (HTS) with recombinantly expressed SARS-CoV-2 Mpro. A fluorescent assay was used to identify inhibitors in a compound library containing known drugs, bioactive molecules and natural products. These screens led to the identification of 13 inhibitors with IC50 values ranging from 0.2 μM to 23 μM. The screens confirmed several known SARS-CoV Mpro inhibitors as inhibitors of SARS-CoV-2 Mpro, such as the organo-mercuric compounds thimerosal and phenylmercuric acetate. Benzophenone derivatives could also be identified among the most potent screening hits. Additionally, Evans blue, a sulfonic acid-containing dye, could be identified as an Mpro inhibitor. The obtained compounds could be of interest as lead compounds for the development of future SARS-CoV-2 drugs.

Synthesis, structural characterization and evaluation of the chelating potential in C. elegans involving complexes of mercury (II) with Schiff bases derived from amino acids

Two series of neutral mercury(II) complexes have been obtained from the reaction of HgPh(OCOCH3)(1, 2, and 3) or Hg(OCOCH3)2(4, 5, and 6) with N-(2-hydroxynaphtalidene)β-alanine (L1H2), N-(5-bromo-salicylidene)β-alanine (L2H2), and N-(5-bromo-salicylidene)β-phenylalanine (L3H2), respectively. The complexes were characterized by elemental analysis, IR, NMR (1H, 13C, and 199Hg) and X-ray crystallography (1 and 2). The elementary analysis showed that the obtained compounds have a high degree of purity and the infrared spectra indicated the shifts of the main functional groups (carboxylate, azomethine and phenol) of the Schiff bases when compared to the respective mercury complexes. X-ray diffraction analyses are similar for complexes 1 and 2, consistent with mononuclear compounds bearing a primarily di-coordinated HgII nucleus with several additional Hg—O interactions, which give rise to supramolecular assemblies. Solution NMR analyses indicate that the primary coordination is retained in DMSO for 1, 2 and 3, but the additional interactions observed in solid state are lost in solution. Complexes 4, 5 and 6 are also mononuclear and all analyses, in both solution and solid state, point to a di-coordinated HgII nucleus with a di-anionic Schiff base ligand. The biological evaluation of the Schiff base (L1H2) chelating potential was performed by pretreating Caenorhabditis elegans (C. elegans) nematodes with the L1H2 (1 mM) followed by phenylmercury acetate exposure (LC50 = 290 μM). The pretreatment with L1H2 resulted in a significant protection of worm survival against phenylmercury acetate toxicity. Together, these data show that the chelating potential of these ligands is a crucial factor in reducing the toxic effects caused by metals in the worm, suggesting them as promising agents in chelation therapy.

Synthesis, Structural Characterization and Evaluation of the Chelating Potential in C. Elegans Involving Complexes of Mercury (Ii) with Schiff Bases Derived from Amino Acids

Two series of neutral mercury(II) complexes have been obtained from the reaction of HgPh(OCOCH 3 )( 1 , 2 , and 3 ) or Hg(OCOCH 3 ) 2 ( 4 , 5 , and 6 ) with N-(2-hydroxynaphtalidene)β-alanine (L1H 2 ), N-(5-bromo-salicylidene)β-alanine (L2H 2 ), and N-(5-bromo-salicylidene)β-phenylalanine (L3H 2 ), respectively. The complexes were characterized by elemental analysis, IR, NMR ( 1 H, 13 C, and 199 Hg) and X-ray crystallography ( 1 and 2 ). X-ray diffraction analyses are similar for complexes 1 and 2 , consistent with mononuclear compounds bearing a primarily di-coordinated Hg II nucleus with several additional Hg—O interactions, which give rise to supramolecular assemblies. Solution NMR analyses indicate that the primary coordination is retained in DMSO for 1 , 2 and 3 , but the additional interactions observed in solid state are lost in solution. Complexes 4 , 5 and 6 are also mononuclear and all analyses, both in solution and solid state, point to a di-coordinated Hg II nucleus with a di-anionic Schiff base ligand. The biological evaluation of the Schiff base (L1H 2 ) chelating potential was performed by pretreating Caenorhabditis elegans ( C. elegans ) nematodes with the L1H 2 (1mM) followed by phenylmercury acetate exposure (LC 50 = 290 μM).The pretreatment with L1H 2 resulted in a significant protection of worm survival against phenylmercury acetate toxicity. Together, these data show that the chelating potential of these ligands is a crucial factor in reducing the toxic effects caused by metals in the worm, suggesting them as promising agents in chelation therapy.

Pseudomonas juntendi sp. nov., isolated from patients in Japan and Myanmar

A Gram-negative, aerobic, rod-shaped, non-spore-forming bacterium, designated as strain BML3T, was isolated from a sputum sample of a hospital patient in Japan. Strain BML3T grew at temperatures from 4 to 40 °C, in 1.0-7.0 % (w/v) NaCl and at pH 6.0-9.0. Results of phylogenetic analysis based on the sequences of housekeeping genes, including the 16S rRNA gene and rpoB, rpoD and gyrB, showed that strain BML3T was part of the Pseudomonas putida group and located close to Pseudomonas asiatica, Pseudomonas monteiliiand P. putida . Whole-genome comparisons, using average nucleotide identity and digital DNA-DNA hybridization, confirmed strain BML3T to be a distinct species among the P. putida group. Phenotypic characterization tests demonstrated that the utilization of phenylmercuric acetate could distinguish this strain from other closed species of the P. putida group. Based on genetic and phenotypic evidence, strain BML3T should be classified as a novel species, for which the name Pseudomonas juntendi sp. nov. is proposed. The type strain is BML3T (=DSM 109244T,=JCM 33395T), with a DNA G+C content of 62.66 mol %.

The leading established metal-based drugs: a revisitation of their relevant physico-chemical data.

The study of metal-based drugs represents an important branch of modern bioinorganic chemistry. The growing importance of this field is linked to the large success in medicine of a few metal based drugs, either in clinical use or still experimental. Moreover, these metal-based drugs are frequently used as reference compounds to assess comparatively the behavior of newly synthesized metallodrugs. For the convenience of researchers working in this area we report here a compilation of the relevant analytical and spectroscopic data of ten representative metallodrugs based on Platinum, Ruthenium, Gold and Mercury. The selected compounds, namely Cisplatin, Oxaliplatin, Carboplatin, Auranofin, Sodium Aurothiomalate, NAMI-A, KP1019, Thimerosal, Merbromin and Phenylmercury Acetate, were chosen owing to their importance in the field. We believe that this compilation may turn very helpful to researchers as these data are difficult to find and generally scattered over a large number of (old) publications.

Molecular forms and fragments of salivary MMP-8 in relation to periodontitis.

To investigate the molecular forms of salivary matrix metalloproteinase (MMP)-8 in relation to periodontitis. Molecular forms, degree of activation and fragmentation of neutrophilic and mesenchymal-type MMP-8 isoforms were analysed from salivary samples of 81 subjects with generalized periodontitis, 63 subjects with localized periodontitis and 79 subjects without pocket teeth, by using western-immunoblots with computer quantitation. In addition, human recombinant proMMP-8 was in vitro activated by Treponema denticola chymotrypsin-like protease (Td-CTLP), sodium hypochlorite (NaOCl, 1mM, oxidant) or amino phenyl mercuric acetate (APMA, 1mM). In saliva of periodontitis-affected individuals, MMP-8 is found in multiple forms, that is, complexes, active and pro-forms of neutrophilic and mesenchymal-type MMP-8, and especially 20-27kDa fragments. The quantity of these fragments was elevated in both localized and generalized forms of periodontitis. Moreover, the tested activators (Td-CTLP, NaOCl and APMA) activated inactive proMMP-8, resulting in fragments of 20-27kDa, in vitro, and salivary concentrations of T.denticola correlated significantly with salivary levels of fragmented MMP-8. The present results indicate that during the development and progression of periodontitis, MMP-8 appears as activated and fragmented, and treponemal proteases most likely play role in this cascade.

Transcriptional responses of Escherichia coli during recovery from inorganic or organic mercury exposure

BackgroundThe protean chemical properties of mercury have long made it attractive for diverse applications, but its toxicity requires great care in its use, disposal, and recycling. Mercury occurs in multiple chemical forms, and the molecular basis for the distinct toxicity of its various forms is only partly understood. Global transcriptomics applied over time can reveal how a cell recognizes a toxicant and what cellular subsystems it marshals to repair and recover from the damage. The longitudinal effects on the transcriptome of exponential phase E. coli were compared during sub-acute exposure to mercuric chloride (HgCl2) or to phenylmercuric acetate (PMA) using RNA-Seq.ResultsDifferential gene expression revealed common and distinct responses to the mercurials throughout recovery. Cultures exhibited growth stasis immediately after each mercurial exposure but returned to normal growth more quickly after PMA exposure than after HgCl2 exposure. Correspondingly, PMA rapidly elicited up-regulation of a large number of genes which continued for 30 min, whereas fewer genes were up-regulated early after HgCl2 exposure only some of which overlapped with PMA up-regulated genes. By 60 min gene expression in PMA-exposed cells was almost indistinguishable from unexposed cells, but HgCl2 exposed cells still had many differentially expressed genes. Relative expression of energy production and most metabolite uptake pathways declined with both compounds, but nearly all stress response systems were up-regulated by one or the other mercurial during recovery.ConclusionsSub-acute exposure influenced expression of ~45% of all genes with many distinct responses for each compound, reflecting differential biochemical damage by each mercurial and the corresponding resources available for repair. This study is the first global, high-resolution view of the transcriptional responses to any common toxicant in a prokaryotic model system from exposure to recovery of active growth. The responses provoked by these two mercurials in this model bacterium also provide insights about how higher organisms may respond to these ubiquitous metal toxicants.

Methylmercury degradation by Pseudomonas putida V1

Environmental contamination of mercury (Hg) has caused public health concerns with focuses on the neurotoxic substance methylmercury, due to its bioaccumulation and biomagnification in food chains. The goals of the present study were to examine: (i) the transformation of methylmercury, thimerosal, phenylmercuric acetate and mercuric chloride by cultures of Pseudomonas putida V1, (ii) the presence of the genes merA and merB in P. putida V1, and (iii) the degradation pathways of methylmercury by P. putida V1. Strain V1 cultures readily degraded methylmercury, thimerosal, phenylmercury acetate, and reduced mercuric chloride into gaseous Hg(0). However, the Hg transformation in LB broth by P. putida V1 was influenced by the type of Hg compounds. The merA gene was detected in P. putida V1, on the other hand, the merB gene was not detected. The sequencing of this gene, showed high similarity (100%) to the mercuric reductase gene of other Pseudomonas spp. Furthermore, tests using radioactive 14C-methylmercury indicated an uncommon release of 14CO2 concomitant with the production of Hg0. The results of the present work suggest that P. putida V1 has the potential to remove methylmercury from contaminated sites. More studies are warranted to determine the mechanism of removal of methylmercury by P. putida V1.

Phenylmercury(ii) sulfanylpropenoates: an example of symmetrization with the 3-(2-methoxyphenyl)-2-sulfanylpropenoato ligand

Some new phenylmercury(ii) sulfanylpropenoate complexes were prepared and characterized. The identification of diphenylmercury(ii) reveals the existence of a symmetrization process, which was followed in solution by NMR.

Richard F. Heck (1931-2015).

Richard F. Heck (1931-2015).

Organic and inorganic mercurials have distinct effects on cellular thiols, metal homeostasis, and Fe-binding proteins in Escherichia coli.

The protean chemical properties of the toxic metal mercury (Hg) have made it attractive in diverse applications since antiquity. However, growing public concern has led to an international agreement to decrease its impact on health and the environment. During a recent proteomics study of acute Hg exposure in E. coli, we also examined the effects of inorganic and organic Hg compounds on thiol and metal homeostases. On brief exposure, lower concentrations of divalent inorganic mercury Hg(II) blocked bulk cellular thiols and protein-associated thiols more completely than higher concentrations of monovalent organomercurials, phenylmercuric acetate (PMA) and merthiolate (MT). Cells bound Hg(II) and PMA in excess of their available thiol ligands; X-ray absorption spectroscopy indicated nitrogens as likely additional ligands. The mercurials released protein-bound iron (Fe) more effectively than common organic oxidants and all disturbed the Na(+)/K(+) electrolyte balance, but none provoked efflux of six essential transition metals including Fe. PMA and MT made stable cysteine monothiol adducts in many Fe-binding proteins, but stable Hg(II) adducts were only seen in CysXxx(n)Cys peptides. We conclude that on acute exposure: (a) the distinct effects of mercurials on thiol and Fe homeostases reflected their different uptake and valences; (b) their similar effects on essential metal and electrolyte homeostases reflected the energy dependence of these processes; and (c) peptide phenylmercury-adducts were more stable or detectable in mass spectrometry than Hg(II)-adducts. These first in vivo observations in a well-defined model organism reveal differences upon acute exposure to inorganic and organic mercurials that may underlie their distinct toxicology.

BLOOD

All forms of mercury are global pollutants having no environmental limits.Human exposure to mercury occurs basically through food chain due to accumulation oforganic forms of mercury in fish. Objectives: The purpose of the present study was to analyzethe effect of phenyl mercuric acetate on plasma and cytosolic fraction GSH. Study Design:Experimental Study. Setting: Department of Pharmaceutical Chemistry, Faculty of Pharmacy,Gomal University, Dera Ismail Khan. Period: 29 January 2011 to 11 march 2012 .StatisticalAnalysis: One-way ANOVA followed by Dunnet’s HSD test. Results: For the estimation ofthiols Ellman’s method was used and was found statistically significant (p < 0.001) decreasein plasma and cytosolic fraction GSH which was dose and time dependent. The plasma GSHcontents drop in 0 to 120 minutes by various concentrations of phenyl mercuric acetate were64.45%, 59.33%, 50.89%, 41.56%, 33.63% and 32.99% while drop in cytosolic fraction GSHlevel from 0 to 120 minutes by different concentrations of phenyl mercuric acetate (PMA) was53.86%, 48.60%, 45.41%, 36.11%, 29.38% and 27.06%.Conclusions: It is clear that duringorganic mercury toxicity the blood components are also affected which is proved from ourresults. With the increase of time ,the mercury toxicity would be more harmful so detoxificationof organic mercury should be done on emergency bases at the earliest with the help of suitablechelating agents along with antioxidant therapy.