@article {770,
	title = {Biolubricant potential of exopolysaccharides from the cyanobacterium Cyanothece epiphytica. [Mass Spectrometry - Glycomics]},
	journal = {Appl Microbiol Biotechnol},
	volume = {102},
	year = {2018},
	month = {2018 Apr},
	pages = {3635-3647},
	abstract = {<p>Exopolysaccaharides (EPS) are carbohydrate polymers secreted by microbial cells, as a protective layer termed sheath or capsule. Their composition is variable. Optimisation of nutrient factors and the effect of some simple stresses on the ability of Cyanothece epiphytica to produce EPS were tested. Of the tested stresses, exposure to ozone for 50\&nbsp;s at 0.06\&nbsp;mg/L resulted in a relatively high EPS yield, without any damage to cell structure. EPS was characterised physicochemically. Chemically, it was found to be composed of pentoses arabinose and xylose; hexoses glucose, galactose and mannose; and the deoxyhexose fucose sugars which were sulphated and with different functional groups. EPS from C. epiphytica was found to be a good hydrophobic dispersant, an excellent emulsifier as well as a flocculant. Its potential as a biolubricant with characteristics better than the conventional lubricant {\textquoteright}grease{\textquoteright} was revealed through analysis. This study gave the clue for developing a commercial technology to produce a less expensive and more environment-friendly natural lubricant from the cyanobacterium C. epiphytica for tribological applications.</p>
},
	issn = {1432-0614},
	doi = {10.1007/s00253-018-8892-x},
	author = {Borah, Dharitri and Nainamalai, Sangeetha and Gopalakrishnan, Subramanian and Rout, Jayashree and Alharbi, Naiyf S and Alharbi, Sulaiman Ali and Nooruddin, Thajuddin}
}
@article {515,
	title = {Biochemical and pharmacological characterization of a toxic fraction and its cytotoxin-like component isolated from Russell{\textquoteright}s viper (Daboia russelii russelii) venom. (Mass Spectrometry)},
	journal = {Comp Biochem Physiol C Toxicol Pharmacol},
	volume = {168},
	year = {2015},
	month = {2015 Feb},
	pages = {55-65},
	abstract = {<p>The pathophysiological significance of a toxic fraction (GF-VI DEAE-II) isolated from Russell{\textquoteright}s viper venom (RVV) is characterized. GF-VI DEAE-II represents 1.6\% of the total RVV protein and it comprises of a 27.6kDa minor component (RP-I) (0.04\%, w/w) and a major 6.6kDa non-enzymatic peptide (1.11\%, w/w), named Rusvitoxin. The LC-MS/MS analysis of RP-I showed its identity to snake venom serine proteases, whereas Rusvitoxin demonstrated its close identity with snake venom three finger toxins, cytotoxins and cardiotoxins particularly from Naja sp. GF-VI DEAE-II was found to be non-cytotoxic to the tested mammalian cancer cells and non-hemolytic; nevertheless, it demonstrated α-fibrin(ogen)ase activity and in vivo toxicity in BALB/c mice with an LD50 (i.p.) of 2.3mg/kg. GF-VI DEAE-II induced lethargy and hind-leg paralysis in mice within 10min of i.p. injection. GF-VI DEAE-II induced hyperfibrinogenomia, and significantly altered (p\&lt;0.05) the plasma levels of factor X, pro- and anti-inflammatory cytokines viz. TNF-α, IL-6 and IL-10 in treated mice. Histological observations of tissues and biochemical properties of serum from GF-VI DEAE-II-treated mice suggested multiple organ dysfunctions. Conversely, Rusvitoxin at a dose of 5mg/kg did not induce toxicity in BALB/c mice. At 1:15 (antigen: antivenom, w/w) ratio, commercially polyvalent and monovalent antivenoms neutralized more than 80\% of the fibrinolytic and anticoagulant activities of GF-VI DEAE-II. The present study suggests the significant role of GF-VI DEAE-II in RVV-induced pathogenesis in victim/prey.</p>
},
	keywords = {Animals, Anticoagulants, Antivenins, Cytotoxins, Fibrinolytic Agents, Interleukin-10, Interleukin-6, Mice, Mice, Inbred BALB C, Mollusk Venoms, Russell{\textquoteright}s Viper, Tumor Necrosis Factor-alpha, Viper Venoms},
	issn = {1532-0456},
	doi = {10.1016/j.cbpc.2014.12.001},
	author = {Thakur, Rupamoni and Chattopadhyay, Pronobesh and Mukherjee, Ashis K}
}
@article {512,
	title = {Biochemistry. Watch water flow.},
	journal = {Science},
	volume = {340},
	year = {2013},
	month = {2013 Jun 14},
	pages = {1294-5},
	keywords = {Aquaporins, Fungal Proteins, Pichia, Water},
	issn = {1095-9203},
	doi = {10.1126/science.1239270},
	author = {Abramson, Jeff (C-CAMP) and Vartanian, Armand S}
}
