| Abstract: | Antibodies were prepared to a chloroplast homolog of the bacterial RNAPase¹ ’-subunit. A fragment of a pea chloroplast homolog of the bacterial rpoC gene, coding for the ’-subunit of RNAPase, was cloned as a translational fusion gene joined to the regulatory region and amino acid terminus of the E. coli anthranilate synthetase (trpE) gene in the expression vector pATH10. A hybrid polypeptide was obtained and used as an antigen to produce rabbit antibodies to the gene product of the rpoC homolog. Purification of the rabbit antiserum showed specific antibodies to the fusion gene product in absence of binding specificity for the trpE-encoded polypeptide. |
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