bacillus subtilis atcc 62037 (ATCC)
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bacillus subtilis atcc 62037
Bacillus Subtilis Atcc 62037, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bacillus+subtilis+atcc+62037/Tetracoccosporium+paxianum+Szabo/pm38242928-49-22-24
Average 94 stars, based on 8 article reviews
Bacillus Subtilis Atcc 62037, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bacillus+subtilis+atcc+62037/Tetracoccosporium+paxianum+Szabo/pm38242928-49-22-24
Average 94 stars, based on 8 article reviews
bacillus subtilis atcc 62037 - by Bioz Stars,
2026-09
94/100 stars
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other:Article Title: Structure-activity relations of parasin I, a histone H2A-derived antimicrobial peptide. Article Snippet: The structure–activity relations and mechanism of action of parasin I, a 19-amino acid histone H2A-derived antimicrobial peptide, were investigated.. Parasin I formed an amphipathic a-helical structure (residues 9–17) flanked by two random coil regions (residues 1–8 and 18–19) in helix-promoting environments.. Deletion of the lysine residue at the Nterminal [Pa(2–19)] resulted in loss of antimicrobial activity, but did not affect the a-helical content of the peptide. Article Title: Helix Stability Confers Salt Resistance upon Helical Antimicrobial Peptides Article Snippet: Microorganisms—The microorganisms used in this study were obtained from the American Type Culture Collection (ATCC) and included: Article Title: Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. Article Snippet: In response to epidermal injury, Parasilurus asotus, a catfish, secreted a strong antimicrobial peptide into the epithelial mucosal layer.. The molecular mass of the antimicrobial peptide, named parasin I, was 2000.4 Da, as determined by matrixassociated laser desorption ionization mass spectrometry.. The complete amino acid sequence of parasin I, which was determined by automated Edman degradation, was Lys-Gly-Arg-Gly-LysGln-Gly-Gly-Lys-Val-Arg-Ala-Lys-Ala-Lys-Thr-Arg-Ser-Ser. Activity Assay:Article Title: High-level expression of an antimicrobial peptide histonin as a natural form by multimerization and furin-mediated cleavage. Article Snippet: Direct expression of an antimicrobial peptide (AMP) in Escherichia coli causes several problems such as the toxicity of AMP to the host cell, its susceptibility to proteolytic degradation, and decreased antimicrobial activity due to the additional residue(s) introduced after cleavage of AMPs from fusion partners.. To overcome these problems and produce a large quantity of a potent AMP histonin (RAGLQFPVGKLLKKLLKRLKR) in E. coli, an efficient expression system was developed, in which the toxicity of histonin was neutralized by a fusion partner F4 (a truncated fragment of PurF protein) and the productivity was increased by a multimeric expression of a histonin gene.. The expression level of the fusion proteins reached a maximum with a 12-mer of a histonin gene. Recombinant:Article Title: High-level expression of an antimicrobial peptide histonin as a natural form by multimerization and furin-mediated cleavage. Article Snippet: Direct expression of an antimicrobial peptide (AMP) in Escherichia coli causes several problems such as the toxicity of AMP to the host cell, its susceptibility to proteolytic degradation, and decreased antimicrobial activity due to the additional residue(s) introduced after cleavage of AMPs from fusion partners.. To overcome these problems and produce a large quantity of a potent AMP histonin (RAGLQFPVGKLLKKLLKRLKR) in E. coli, an efficient expression system was developed, in which the toxicity of histonin was neutralized by a fusion partner F4 (a truncated fragment of PurF protein) and the productivity was increased by a multimeric expression of a histonin gene.. The expression level of the fusion proteins reached a maximum with a 12-mer of a histonin gene. Bacteria:Article Title: High-level expression of an antimicrobial peptide histonin as a natural form by multimerization and furin-mediated cleavage. Article Snippet: Direct expression of an antimicrobial peptide (AMP) in Escherichia coli causes several problems such as the toxicity of AMP to the host cell, its susceptibility to proteolytic degradation, and decreased antimicrobial activity due to the additional residue(s) introduced after cleavage of AMPs from fusion partners.. To overcome these problems and produce a large quantity of a potent AMP histonin (RAGLQFPVGKLLKKLLKRLKR) in E. coli, an efficient expression system was developed, in which the toxicity of histonin was neutralized by a fusion partner F4 (a truncated fragment of PurF protein) and the productivity was increased by a multimeric expression of a histonin gene.. The expression level of the fusion proteins reached a maximum with a 12-mer of a histonin gene. Microdilution Assay:Article Title: High-level expression of an antimicrobial peptide histonin as a natural form by multimerization and furin-mediated cleavage. Article Snippet: Direct expression of an antimicrobial peptide (AMP) in Escherichia coli causes several problems such as the toxicity of AMP to the host cell, its susceptibility to proteolytic degradation, and decreased antimicrobial activity due to the additional residue(s) introduced after cleavage of AMPs from fusion partners.. To overcome these problems and produce a large quantity of a potent AMP histonin (RAGLQFPVGKLLKKLLKRLKR) in E. coli, an efficient expression system was developed, in which the toxicity of histonin was neutralized by a fusion partner F4 (a truncated fragment of PurF protein) and the productivity was increased by a multimeric expression of a histonin gene.. The expression level of the fusion proteins reached a maximum with a 12-mer of a histonin gene. |