ena-STUDY-VIT-16-09-2013-06:41:33:545-22
Enzymes for clot busting
According to world health organisation cardiovascular disease caused over 18 million  deaths in the world in 2005. Of these deaths 8 million (44%) occurred in people in 60 years of   age. In recent years, of the several thrombolytic agents used clinically, Nattokinase (NK) is most   often employed, particularly of its low cost and its producing feasibility when compared with   other thrombolytic agents. NK was produced from the  Pseudomonas aeruginosa which was   isolated from the Fresian cow milk and throat samples. The enzyme production was optimised   and then the enzyme was purified using ammonium sulphate precipitation, dialysis, DEAEDi Ethyl Amino Ethylene Cellulose and affinity chromatography. Molecular weight of NK   (29kDa) was confirmed using SDS-PAGE. The Crystallographic structure of  Pseudomonas   aeruginosa  NK is an striking target for designing the thrombolytic agent. For this cause we   report a computer based homology study conducted to build its three dimensional structure   which was based on the amino acid sequence of this enzyme. In this study the enzyme residues   was read using PDB(proteinData Bank) and rough model of the enzyme was generated using   MODELLER 9.0. The protein (enzyme) quality was checked using Ramachandran plot. Active   site was read using PATCH DOCK tool.
According to world health organisation cardiovascular disease caused over 18 million  deaths in the world in 2005. Of these deaths 8 million (44%) occurred in people in 60 years of   age. In recent years, of the several thrombolytic agents used clinically, Nattokinase (NK) is most   often employed, particularly of its low cost and its producing feasibility when compared with   other thrombolytic agents. NK was produced from the  Pseudomonas aeruginosa which was   isolated from the Fresian cow milk and throat samples. The enzyme production was optimised   and then the enzyme was purified using ammonium sulphate precipitation, dialysis, DEAEDi Ethyl Amino Ethylene Cellulose and affinity chromatography. Molecular weight of NK   (29kDa) was confirmed using SDS-PAGE. The Crystallographic structure of  Pseudomonas   aeruginosa  NK is an striking target for designing the thrombolytic agent. For this cause we   report a computer based homology study conducted to build its three dimensional structure   which was based on the amino acid sequence of this enzyme. In this study the enzyme residues   was read using PDB(proteinData Bank) and rough model of the enzyme was generated using   MODELLER 9.0. The protein (enzyme) quality was checked using Ramachandran plot. Active   site was read using PATCH DOCK tool.