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The present study aimed to investigate the enzymetic, non-enzymetic toxicity and antioxidant potential of a drug candidate 5-Benzyl-1,3,4-Oxadiazole-2-Thiol(OXPA) using computational tools and in vivo models. The binding pattern of it, with different toxicity/oxidative enzymes was predicted using software pkCSM, Protox- II, LAZAR, Mcule 1-Click Docking 3D-Ligand binding Site and best score obtained used as an evaluating criterion. After acute oral toxicity, in vivo.

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Engineering the bioelectrochemical interface using functional nanomaterials and microchip technique toward sensitive and portable electrochemical biosensors.

Biosens Bioelectron

February 2016

State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, China. Electronic address:

Electrochemical biosensors have played active roles at the forefront of bioanalysis because they have the potential to achieve sensitive, specific and low-cost detection of biomolecules and many others. Engineering the electrochemical sensing interface with functional nanomaterials leads to novel electrochemical biosensors with improved performances in terms of sensitivity, selectivity, stability and simplicity. Functional nanomaterials possess good conductivity, catalytic activity, biocompatibility and high surface area.

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[Enzymetic synthesis and characterization of a carnosine analogue in non-aqueous solvent].

Sheng Wu Gong Cheng Xue Bao

December 2009

College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030, China.

Carnosine (beta-Ala-L-His) has high antioxidant activity, and it is widely used in biology, chemical engineering, medicine and other fields. Its analogue syntheised in non-aqueous solvent and catalyzed by enzymes is high-effective but low-price, so it has great prospect. Here, we synthesized a carnosine analogue imidazole 4(5)-alanylamide-5(4)-carboxylic acid with imidazole-4,5-dicarboxylic acid and L-Alanine as substrates, alpha-chymotrypsin as catalyst in tetrahydrofuran (THF) solvent.

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[6A8 alpha-mannosidase catalyzes p-nitrophenyl-alpha-D-mannopyranoside].

Zhongguo Yi Xue Ke Xue Yuan Xue Bao

October 2001

Department of Immunology, Institute of Basic Medical Sciences, CAMS, PUMC, Beijing 100005, China.

Objective: To confirm the alpha-mannosidase nature of the protein encoded by 6A8 cDNA.

Methods: 1) To construct a full-length 6A8 cDNA based on the three cloned DNA fragments by means of gene recombinant technique; 2) To insert the 6A8 cDNA into eukaryotic expression vector pCDI; 3) To transfect the recombinant pCDI-6A8 into COS-7 cells; 4) To characterize the nature of the protein encoded by 6A8 cDNA by means of enzymic activity assay and Western blotting assay.

Results: The constructed 6A8 cDNA was the right cDNA in sequence.

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Objective: To construct the eukáryotic expression recombinant plasmid, pcIFN-gamma, as a genetic adjuvant and observe the immune responses elicited by pcDNA3-rhoptry protein 1 (pc-ROP1) combined with pcIFN-gamma against Toxoplasma gondii (T. gondii) infection in mice.

Methods: A fragment of the IFN-gamma gene was directly inserted into the pcDNA3 plasmid and identified by two restriction endonucleases digestion.

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