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31.
Identification of emissive lanthanide complexes suitable for cellular imaging that resist quenching by endogenous anti-oxidants 总被引:1,自引:0,他引:1
Poole RA Montgomery CP New EJ Congreve A Parker D Botta M 《Organic & biomolecular chemistry》2007,5(13):2055-2062
Excited state quenching by urate and ascorbate of selected europium and terbium(III) macrocyclic complexes has been assessed and related to the ease of complex visualisation by optical microscopy inside various living cells, e.g. CHO, COS and NIH 3T3. It is the relative insensitivity of certain sterically encumbered complexes to dynamic quenching by urate that favours their usage for in cellulo applications. Non-covalent binding of the complex by protein also shields the excited lanthanide(III) ion from collisional quenching; this effect is most marked for a cationic triamide complex, [Ln.1](3+), consistent with its ease of visualisation by luminescence microscopy. 相似文献
32.
Kielar F Congreve A Law GL New EJ Parker D Wong KL Castreno P de Mendoza J 《Chemical communications (Cambridge, England)》2008,(21):2435-2437
An emissive terbium complex has been conjugated to a C12 chain, Lys-Arg7, Arg7, a tetraguanidinium cation and human serum albumin; two-photon excitation at 720 nm facilitated microscopy studies revealing cell localisation profiles with the oligo-guanidinium conjugate localising in mitochondria but causing apoptotic cell death (IC(50)12 microM), the C12-amide complex giving rise to necrotic cell death in skin fibroblasts (IC50 8 microM) and the peptide conjugates and the methyl ester generating punctuate cytosolic intracellular distributions. 相似文献
33.
Helane?MS?Costa Augusto?CV?Freitas Júnior Ian?PG?Amaral Izaura?Y?Hirata Patrícia?MG?Paiva Luiz?B?CarvalhoJr Vitor?Oliveira Ranilson?S?BezerraEmail author 《Chemistry Central journal》2013,7(1):166
Background
Over the past decades, the economic development and world population growth has led to increased for food demand. Increasing the fish production is considered one of the alternatives to meet the increased food demand, but the processing of fish leads to by-products such as skin, bones and viscera, a source of environmental contamination. Fish viscera have been reported as an important source of digestive proteases with interesting characteristics for biotechnological processes. Thus, the aim of this study was to purify and to characterize a trypsin from the processing by-products of crevalle jack (Caranx hippos) fish.Results
A 27.5 kDa trypsin with N-terminal amino acid sequence IVGGFECTPHVFAYQ was easily purified from the pyloric caeca of the crevalle jack. Its physicochemical and kinetic properties were evaluated using N-α-benzoyl-DL-arginine-p-nitroanilide (BApNA) as substrate. In addition, the effects of various metal ions and specific protease inhibitors on trypsin activity were determined. Optimum pH and temperature were 8.0 and 50°C, respectively. After incubation at 50°C for 30 min the enzyme lost only 20% of its activity. K m , kcat, and k cat /K m values using BApNA as substrate were 0.689 mM, 6.9 s-1, and 10 s-1 mM-1, respectively. High inhibition of trypsin activity was observed after incubation with Cd2+, Al3+, Zn2+, Cu2+, Pb2+, and Hg2+ at 1 mM, revealing high sensitivity of the enzyme to metal ions.Conclusions
Extraction of a thermostable trypsin from by-products of the fishery industry confirms the potential of these materials as an alternative source of these biomolecules. Furthermore, the results suggest that this trypsin-like enzyme presents interesting biotechnological properties for industrial applications.34.
Sandip N.Gavade Ravi S.Balaskar Madhav S.Mane Pramod N.Pabrekar Murlidhar S.Shingare Dhananjay V.Mane 《中国化学快报》2011,22(6):675-678
The coupling reaction of phenylurea with different functionalized aryl halides in the presence of air stable CuI,N,N-dimethylethylenediamine as a ligand,and K3PO4 as a base gives symmetrical and unsymmetrical diarylureas in relatively high yields.This method is milder than the palladium catalyzed arylation and avoids the use of toxic phosphine ligands. 相似文献