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Abstract
Nicotiana tabacum was transformed with a gene encoding anti-PreS1 of hepatitis B surface antigen single-chain Fv antibody (scFv) and bearing an N-terminal endoplasmic reticulum protein signal peptide sequence. The scFv antibody protein was continuously secreted from the transgenic tobacco roots into a simple hydroponic medium at 630 to 760 ng g^sup -1^ dry wt root day^sup -1^. The antibody was about 2% of the total secreted protein and still possessed antigen-binding activity.[PUBLICATION ABSTRACT]





