Abstract
With the α-amylase promoter and ribosome binding site, Bacillis subtilis was used to express the sweet plant protein thaumatin II cDNA fused in the correct reading frame to the α-amylase leader peptide. The r-thaumatin was purified from the medium on a S-Sepharose column and detected with western blots by sheep α-thaumatin antibodies. The r-thaumatin and authentic thaumatin were the same size when reduced by 2-ME and the same size when not reduced.
Original language | English (US) |
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Pages (from-to) | 587-592 |
Number of pages | 6 |
Journal | Biotechnology Letters |
Volume | 10 |
Issue number | 8 |
DOIs | |
State | Published - Aug 1988 |