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An Efficient Synthesis of 2-Alkyl-4-hydroxy-2H-1,2-benzothiazine-3-carboxamide-1,1-dioxides
Zia ur Rehman, Muhammad,Choudary, Jamil Anwar,Ahmad, Saeed Korean Chemical Society 2005 Bulletin of the Korean Chemical Society Vol.26 No.11
An efficient and environment friendly method has been described for the synthesis of various 2-alkyl-4-hydroxy-2H-1,2-benzothiazine-3-carboxamide-1,1-dioxides starting from N-alkylation of sodium obenzosulfimide in an ionic liquid for the first time. Ring cleavage and ring closure of the resulting product were achieved in a single step in a cost effective solvent (methanol) followed by N-alkylation of resulting alkyl 4-hydroxy-2H-1,2-benzothiazine-3-carboxylate in ionic liquid while boron triflouride was used as a catalyst along with molecular sieves in carboxamide formation step.
An Efficient Synthesis of 2-Alkyl-4-hydroxy-2H-1,2-benzothiazine-3-carboxamide-1,1-dioxides
Muhammad Zia-ur-Rehman,Jamil Anwar Choudary,Saeed Ahmad 대한화학회 2005 Bulletin of the Korean Chemical Society Vol.26 No.11
An efficient and environment friendly method has been described for the synthesis of various 2-alkyl-4-hydroxy-2H-1,2-benzothiazine-3-carboxamide-1,1-dioxides starting from N-alkylation of sodium o-benzosulfimide in an ionic liquid for the first time. Ring cleavage and ring closure of the resulting product were achieved in a single step in a cost effective solvent (methanol) followed by N-alkylation of resulting alkyl 4-hydroxy-2H-1,2-benzothiazine-3-carboxylate in ionic liquid while boron triflouride was used as a catalyst along with molecular sieves in carboxamide formation step.
Jin, Byung Rae,Yoon, Hyung Joo,Kang, Seok Kwon,Choudary, Prabhakara V. 東亞大學校附設遺傳工學硏究所 1998 遺傳工學硏究 Vol.- No.5
Genomic DNA of recombinant AcNPV expressing B-galactosidase was cotransfected with p143helicase gene of BmNPV into Sf21 celis. Ac-Bm hybrid viruses capable of replicating in both Bm5 and Sf21 cells were isolated. Ac-Bm hybrid viruses expressing B-galactosidase either at the highest (Ac-Bm hybrid virus-HE) or lowest (Ac-Bm hybrid virus-LE) level were chosen for the characterization of B-galactosidase expression in Bm5 and Sf21 cells. Expression level of B-galactosidase and replication of Ac-Bm hybrid virus-He in Sf21 cells were nearly identical to those of recombinant AcNPV. Furthermore, replication of Ac-Bm hybrid virus-HE in Bm5 cells was similar to that of wild-type BmNPV, and Ac-Bm hybrid virus-HE clearly expressed B-galactosidase in Bm5 cells. However, expression of B-galactosidase by Ac-Bm hybrid virus-HE in Bm5 cells was significantly lower than that expressed in Sf21 cells. The titer or Ac-Bm hybrid virus-HE determined by plaque assays in Bm5 cells was similar to that determined in Sf21 cells, but the plaque size formed by Ac-Bm hybrid virus-HE in Bm5 cells was apparently smaller than that formed in Sf21 cells. In addition, expression levels and virus titers of Ac-Bm hybrid virus-LE in Sf21 and Bm5 were significantly lower than those of Ac-Bm hybrid virus-HE. Therefore, DNA sequences were determined for the region of the p143 gene controlling the host range in Ac-Bm hybrid viruses. The results showed that the deduced amino acid sequences of Ac-Bm hybrid virus-LE were different at position 461, 470, 514, and 528 from those of BmNPV. In conclusion, our results clearly demonstrated that Ac-Bm hybrid virus-HE has an additional advantage of expanded host range for producing recombinant proteins.