2015
DOI: 10.1016/s2095-3119(14)60950-3
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Comparison and optimization of the method for Cry1Ac protoxin preparation in HD73 strain

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Cited by 19 publications
(16 citation statements)
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“…He obtained Cry1Ac protoxin by growing the HD73 strain of Bt subsp. kurstaki in 1/2 Luria-Bertani medium using the repeated crystal solubilization method 59 . In the first and second sets of bioassays, we compared Cry1Ac protoxin with trypsin-activated Cry1Ac purchased from Marianne Pusztai-Carey that she produced as described above.…”
Section: Methodsmentioning
confidence: 99%
“…He obtained Cry1Ac protoxin by growing the HD73 strain of Bt subsp. kurstaki in 1/2 Luria-Bertani medium using the repeated crystal solubilization method 59 . In the first and second sets of bioassays, we compared Cry1Ac protoxin with trypsin-activated Cry1Ac purchased from Marianne Pusztai-Carey that she produced as described above.…”
Section: Methodsmentioning
confidence: 99%
“…The Cry1Ab/1Ac fusion gene was driven by the promoter of Cry1Ac gene and the construct was expressed in Bt HD73-strain. The recombinant protein was extracted as described previously by Zhou et al (2015). The protoxin was incubated with trypsin (2 mg per 100 mg of protoxin) at 37 C for 3 h, and the 66 kDa fusion protein was generated.…”
Section: Test Materialsmentioning
confidence: 99%
“…B. thuringiensis strain Biot1Ah, carrying the cry1Ah1 gene (21), was grown in 0.5ϫ LB medium at 220 rpm and 30°C until sporulation. Cry1Ah protoxin was prepared using repeated crystal solubilization methods as described previously (42). Cry1Ah protoxin was digested by trypsin at a 20:1 mass ratio (protein to trypsin) at 37°C for 2 h. The activated Cry1Ah toxin was purified by size exclusion chromatography (Superdex 75 10/300, AKTA Avant; GE Healthcare, Uppsala, Sweden) using phosphate-buffered saline (PBS) buffer at a 1-ml/min flow rate.…”
Section: Methodsmentioning
confidence: 99%