Phenol, an aromatic chemical commonly found in domestic and industrial effluents, upon its introduction into aquatic ecosystems adversely affects the indigenous biota, the invertebrates and the vertebrates. With the increased demand for agrochemicals, a large amount of phenol is released directly into the environment as a byproduct. Phenol and its derivatives tend to persist in the environment for longer periods which in turn poses a threat to both humans and the aquatic ecosystem. In our current study, the response of Labeo rohita to sublethal concentrations of phenol was observed and the results did show a regular decrease in biochemical constituents of the targeted organs. Exposure of Labeo rohita to sublethal concentration of phenol (22.32 mg/L) for an epoch of 7, 21 and 28 days shows a decline in lipid, protein, carbohydrate content and phosphatase activity in target organs such as the gills, muscle, intestine, liver and kidney of the fish. The present study also aims to investigate the toxic effects of phenol with special reference to the haematological parameters of Labeo rohita. At the end of the exposure period, the blood of the fish was collected by cutting the caudal peduncle with a surgical scalpel. And it was observed that the red blood corpuscle count (RBC), white blood corpuscle (WBC), haemoglobin count (Hb), packed cell volume (PCV), mean corpuscular volume (MCV), mean corpuscular haemoglobin (MCH) and mean corpuscular haemoglobin concentration (MCHC) values showed a decline after exposure to phenol for 7 days, while white blood corpuscle (WBC) shows an increased count. At 21 days and 28 days, all the haematological parameters showed a significant decrease.
1. The biological properties of twelve samples of venoms from all four species of Dendroaspis (mamba) were investigated. 2. Dendroaspis venoms generally exhibited very low levels of protease, phosphodiesterase and alkaline phosphomonoesterase; low to moderately low level of 5'-nucleotidase and very high hyaluronidase activities, but were devoid of L-amino acid oxidase, phospholipase A, acetylcholinesterase and arginine ester hydrolase activities. The unusual feature in venom enzyme content can be used to distinguish Dendroaspis venoms from other snake venoms. 3. All Dendroaspis venoms did not exhibit hemorrhagic or procoagulant activity. Some Dendroaspis venoms, however, exhibited strong anticoagulant activity. The intravenous median lethal dose of the venoms ranged from 0.5 microgram/g mouse to 4.2 micrograms/g mouse. 4. Venom biological activities are not very useful for the differentiation of the Dendroaspis species. The four Dendroaspis venoms, however, can be differentiated by their venom SDS-polyacrylamide gel electrophoretic patterns.
To evaluate the potential role of extracellular proteins in the pathogenicity and virulence of Burkholderia pseudomallei, the activities of several enzymes in the culture filtrates of nine clinical and six environmental isolates were investigated in vitro and in vivo in ICR strain of mice. The production of protease, phosphatase, phospholipase C, superoxide dismutase, catalase and peroxidase were detected in the culture filtrates of all the 15 isolates at different time points of growth 4-24h. Over time, activity of each enzyme at each time point varied. Profile of secretion was similar among the 15 isolates irrespective of source, that is clinical or environmental. Catalase, phosphatase and phospholipase C were found to be increased in 60-100% of the isolates post-passage in mice. In vivo inoculation studies in ICR mice demonstrated a wide difference in their ability to cause bacteraemia, splenic or external abscesses and mortality rate ranged from few days to several weeks.
1. The hemorrhagic, procoagulant, anticoagulant, phosphodiesterase, alkaline phosphomonoesterase, 5'-nucleotidase, hyaluronidase, arginine ester hydrolase, phospholipase A, L-amino acid oxidase and protease activities of 31 samples of venom from three species of Agkistrodon (A. bilineatus, A. contortrix and A. piscivorus) and 10 venom samples from five other related species belonging to the same tribe of Agkistrodontini were examined. 2. The results indicate that interspecific differences in certain biological activities of the Agkistrodon venoms are more marked than individual variations of the activities, and that these differences can be used for differentiation of the species. Particularly useful for this purpose are the phosphodiesterase, arginine ester hydrolase and anticoagulant activities of the venoms. 3. Venoms of the subspecies of A. contortrix and A. piscivorus do not differ significantly in their biological activities.
The Malayan pit viper (Calloselasma rhodostoma) is of major clinical significance both as a leading cause of snakebite and as the source of ancrod (Arvin). Although its venom has been extensively studied, the degree to which venom composition varies between individuals is poorly known. We individually analysed the venoms of over 100 C. rhodostoma using isoelectric focusing. In all populations, females produced an intense band that was absent from all males, and significant ontogenetic variation was detected. Principal components analysis of the banding profiles also revealed strong geographic variation, which was significantly congruent with variation in the biological activities of the venom (phosphodiesterase, alkalinephosphoesterase, L-amino acid oxidase, arginine ester hydrolase, 5'-nucleotidase, thrombin-like enzyme, haemorrhagic activity). Studies of captive-bred snakes indicate that the intraspecific variation in venom is genetically inherited rather than environmentally induced. The intraspecific variation in venom composition and biological activity could be of applied importance to snakebite therapy, both in correct diagnosis of the source of envenomation and in the development of a more effective antivenom. Greater attention should be given to the source of C. rhodostoma venom used in research to ensure reproducibility of results.
MTH1 is an enzyme that hydrolyzes 8-oxo-dGTP, which is an oxidatively damaged nucleobase, into 8-oxo-dGMP in nucleotide pools to prevent its mis-incorporation into genomic DNA. Selective and potent MTH1-binding molecules have potential as biological tools and drug candidates. We recently developed 8-halogenated 7-deaza-dGTP as an 8-oxo-dGTP mimic and found that it was not hydrolyzed, but inhibited enzyme activity. To further increase MTH1 binding, we herein designed and synthesized 7,8-dihalogenated 7-deaza-dG derivatives. We successfully synthesized multiple derivatives, including substituted nucleosides and nucleotides, using 7-deaza-dG as a starting material. Evaluations of the inhibition of MTH1 activity revealed the strong inhibitory effects on enzyme activity of the 7,8-dihalogenated 7-deaza-dG derivatives, particularly 7,8-dibromo 7-daza-dGTP. Based on the results obtained on kinetic parameters and from computational docking simulating studies, these nucleotide analogs interacted with the active site of MTH1 and competitively inhibited the substrate 8-oxodGTP. Therefore, novel properties of repair enzymes in cells may be elucidated using new compounds.