The Experts below are selected from a list of 552 Experts worldwide ranked by ideXlab platform
Flavia Marinelli - One of the best experts on this subject based on the ideXlab platform.
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Biotransformation of the lipoglycopeptide antibiotic A40926 byActinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced by Actinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria and Neisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells of Actinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L^−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished with tert -butoxycarbonyl ( tert -BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
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Biotransformation of the lipoglycopeptide antibiotic A40926 by Actinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced byActinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria andNeisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells ofActinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished withtert-butoxycarbonyl (tert-BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
A. Carelli - One of the best experts on this subject based on the ideXlab platform.
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Biotransformation of the lipoglycopeptide antibiotic A40926 byActinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced by Actinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria and Neisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells of Actinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L^−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished with tert -butoxycarbonyl ( tert -BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
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Biotransformation of the lipoglycopeptide antibiotic A40926 by Actinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced byActinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria andNeisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells ofActinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished withtert-butoxycarbonyl (tert-BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
Zong Hong - One of the best experts on this subject based on the ideXlab platform.
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Construction of eucaryotic expression vector of T-cell receptor γV_1 and its expression
Journal of Zhengzhou University, 2004Co-Authors: Zong HongAbstract:Aim: To construct the eucaryotic expression vector of TCRγV 1 and to express recombinant TCRγV 1 in skeletal muscle of rats. Methods: The RNA of TCRγV 1 was extracted from human Jurkat cells. TCRγV 1 gene containing BamHI and HindⅢ Endoenzyme sites was obtained by using RT-PCR method. The expressing plasmid pcDNA3 and TCRγV 1 gene were cleaved with 2 restriction endonuclease BamH Ⅰ and Hind Ⅲ. Both fragments were connected by using ligase and transformed into bacteria DH5α. The colonies were scrmoriseeened and the recombinant was sequenced for identification.A large quantity of plasmids were extracted. The recombinant plasmids were injected in bilateral quadriceps femorises of BALB/c rats. The mRNA expression of recombinant plasmids was tested with RT-PCR method.Results: The eucaryotic expression vector pcDNA3/TCRγV 1 was constructed and its mRNA was expressed in the muscle of BALB/c rats after being immunized. Conclusion: The eucaryotic expression vector pcDNA3/TCRγV 1 has been construted and the mRNA of TCRγV 1 could express in skeletal muscle of immunized rats.
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Construction of T-cell Receptor γV_1 Rearrangement Gene Expression Vector in Eucaryotic Cells
Henan Journal of Oncology, 2003Co-Authors: Zong HongAbstract:Objective This study was designed to construct the eucaryotic expression vector of TCRγV_1 rearrangement gene.Methods TCRγV_1 rearrangement gene containing Xba I and BglII Endoenzyme sites was obtained using PCR ;double enzyme digestion was conducted for vector VR1012 and PCR product of TCRγV_1 gene; Both fragments were connected using ligase and transferred to E.coli-DH5α ; Reconstitute plasmid sequence was examined by auto-sequencing assay and was named as VR1012/TCRγ. Conclusion Reconstitution of VR1012/TCRγ vector lay a foundation for T-cell lymphoma gene therapy .
Angelo Borghi - One of the best experts on this subject based on the ideXlab platform.
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Biotransformation of the lipoglycopeptide antibiotic A40926 byActinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced by Actinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria and Neisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells of Actinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L^−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished with tert -butoxycarbonyl ( tert -BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
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Biotransformation of the lipoglycopeptide antibiotic A40926 by Actinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced byActinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria andNeisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells ofActinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished withtert-butoxycarbonyl (tert-BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
Lucia Carrano - One of the best experts on this subject based on the ideXlab platform.
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Biotransformation of the lipoglycopeptide antibiotic A40926 byActinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced by Actinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria and Neisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells of Actinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L^−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished with tert -butoxycarbonyl ( tert -BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.
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Biotransformation of the lipoglycopeptide antibiotic A40926 by Actinoplanes teichomyceticus cells
Journal of Industrial Microbiology, 1995Co-Authors: A. Carelli, Angelo Borghi, Lucia Carrano, Luciano Gastaldo, Flavia MarinelliAbstract:Compound A40926, produced byActinomadura ATCC 39727, is a lipoglycopeptide antibiotic complex which inhibits Gram-positive bacteria andNeisseria species. Individual components of the complex have an identical glycopeptide core but differ in the acid chains attached to the amino group of the glucuronic moiety. Suspension cultures and resting cells ofActinoplanes teichomyceticus ATCC 31121 were able to deacylate compound A40926 factors to yield the glycopeptide nucleus, which can be then synthetically reacylated to form new analogs. In an optimized fedbatch deacylation process, 0.5 g L−1 of compound A40926 was almost completely converted into the deacyl derivative. Under the same conditions, deacylation was also accomplished withtert-butoxycarbonyl (tert-BOC) A40926, in which the amino group at C15 was blocked to prevent formation of diacyl analogs during reacylation. The deacylase is an Endoenzyme whose preliminary characterization is presented.