Abstract
Our previous work showed that the crystal protein of Bacillus thuringiensis var. tolworth, a highly potent toxin for Lepidopteran larvae consists of two polypeptide components of molecular weights 55000 (“component A”) and 120000 (“component B”) in the molar ratio 2:1. In this study we demonstrate by several criteria that A and B are synthesized de novo, synchronously, for a predetermined and relatively brief period, during the 24‐h growth cycle in culture, about 17 h after innoculation of the culture, midway between the cessation of growth and cell lysis. This conclusion is supported by the results of the following types of experiments: 1. pulse‐labelling of cultures of B. thuringiensis with radioactive amino acids and subsequent analysis of the radioactivity in the separated crystal protein components; 2. antigenic analysis of protein isolated from cultures at different times, both by precipitin reactions and immunodiffusion in Ouchterlony plates, using antiserum against purified crystal protein and 3. bioassay of the toxicity of similar protein preparations to the larvae of Pieris brassicae.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
